\\n\\n
Dr. Pletser’s experience includes 30 years of working with the European Space Agency as a Senior Physicist/Engineer and coordinating their parabolic flight campaigns, and he is the Guinness World Record holder for the most number of aircraft flown (12) in parabolas, personally logging more than 7,300 parabolas.
\\n\\nSeeing the 5,000th book published makes us at the same time proud, happy, humble, and grateful. This is a great opportunity to stop and celebrate what we have done so far, but is also an opportunity to engage even more, grow, and succeed. It wouldn't be possible to get here without the synergy of team members’ hard work and authors and editors who devote time and their expertise into Open Access book publishing with us.
\\n\\nOver these years, we have gone from pioneering the scientific Open Access book publishing field to being the world’s largest Open Access book publisher. Nonetheless, our vision has remained the same: to meet the challenges of making relevant knowledge available to the worldwide community under the Open Access model.
\\n\\nWe are excited about the present, and we look forward to sharing many more successes in the future.
\\n\\nThank you all for being part of the journey. 5,000 times thank you!
\\n\\nNow with 5,000 titles available Open Access, which one will you read next?
\\n\\nRead, share and download for free: https://www.intechopen.com/books
\\n\\n\\n\\n
\\n"}]',published:!0,mainMedia:null},components:[{type:"htmlEditorComponent",content:'
Preparation of Space Experiments edited by international leading expert Dr. Vladimir Pletser, Director of Space Training Operations at Blue Abyss is the 5,000th Open Access book published by IntechOpen and our milestone publication!
\n\n"This book presents some of the current trends in space microgravity research. The eleven chapters introduce various facets of space research in physical sciences, human physiology and technology developed using the microgravity environment not only to improve our fundamental understanding in these domains but also to adapt this new knowledge for application on earth." says the editor. Listen what else Dr. Pletser has to say...
\n\n\n\nDr. Pletser’s experience includes 30 years of working with the European Space Agency as a Senior Physicist/Engineer and coordinating their parabolic flight campaigns, and he is the Guinness World Record holder for the most number of aircraft flown (12) in parabolas, personally logging more than 7,300 parabolas.
\n\nSeeing the 5,000th book published makes us at the same time proud, happy, humble, and grateful. This is a great opportunity to stop and celebrate what we have done so far, but is also an opportunity to engage even more, grow, and succeed. It wouldn't be possible to get here without the synergy of team members’ hard work and authors and editors who devote time and their expertise into Open Access book publishing with us.
\n\nOver these years, we have gone from pioneering the scientific Open Access book publishing field to being the world’s largest Open Access book publisher. Nonetheless, our vision has remained the same: to meet the challenges of making relevant knowledge available to the worldwide community under the Open Access model.
\n\nWe are excited about the present, and we look forward to sharing many more successes in the future.
\n\nThank you all for being part of the journey. 5,000 times thank you!
\n\nNow with 5,000 titles available Open Access, which one will you read next?
\n\nRead, share and download for free: https://www.intechopen.com/books
\n\n\n\n
\n'}],latestNews:[{slug:"stanford-university-identifies-top-2-scientists-over-1-000-are-intechopen-authors-and-editors-20210122",title:"Stanford University Identifies Top 2% Scientists, Over 1,000 are IntechOpen Authors and Editors"},{slug:"intechopen-authors-included-in-the-highly-cited-researchers-list-for-2020-20210121",title:"IntechOpen Authors Included in the Highly Cited Researchers List for 2020"},{slug:"intechopen-maintains-position-as-the-world-s-largest-oa-book-publisher-20201218",title:"IntechOpen Maintains Position as the World’s Largest OA Book Publisher"},{slug:"all-intechopen-books-available-on-perlego-20201215",title:"All IntechOpen Books Available on Perlego"},{slug:"oiv-awards-recognizes-intechopen-s-editors-20201127",title:"OIV Awards Recognizes IntechOpen's Editors"},{slug:"intechopen-joins-crossref-s-initiative-for-open-abstracts-i4oa-to-boost-the-discovery-of-research-20201005",title:"IntechOpen joins Crossref's Initiative for Open Abstracts (I4OA) to Boost the Discovery of Research"},{slug:"intechopen-hits-milestone-5-000-open-access-books-published-20200908",title:"IntechOpen hits milestone: 5,000 Open Access books published!"},{slug:"intechopen-books-hosted-on-the-mathworks-book-program-20200819",title:"IntechOpen Books Hosted on the MathWorks Book Program"}]},book:{item:{type:"book",id:"6537",leadTitle:null,fullTitle:"Evolving Strategies in Peritoneal Dialysis",title:"Evolving Strategies in Peritoneal Dialysis",subtitle:null,reviewType:"peer-reviewed",abstract:"Evolving Strategies in Peritoneal Dialysis is intended as a concise compilation of articles designed to understand the basics of the current practice of the most cost-effective form of life support for patients with end-stage renal disease who require dialysis. Current strategies are understood best with a review of the historical development of catheter materials, solution packaging, and simplified machinery, which allow safe and effective nocturnal treatments. Quantitation of the efficacy of peritoneal dialysis is also reviewed because such calculations were also developed by the pioneers of nephrology to ensure adequacy of dialysis and daily fluid balance, which are responsible for the best chance for long-term patient survival. Comparison of methods for catheter placement is presented as well as the role that a dialysis center plays in the health and success of this form of end-stage renal disease patient care. The novel concept of assisted peritoneal dialysis for the infirm or institutionalized patients is probably the next direction needed to make available this treatment to many more patients than are currently eligible to receive it. This concept is explored in a separate chapter. Finally, professional dialysis staff must monthly assess individuals' nutritional status, bone health, and infection prevention and treatment to ensure the greatest functional status for these patients. This book concludes with a review of each of these topics to expand the mandatory monthly surveillance performed by dialysis centers for each patient who receives home peritoneal dialysis therapy.",isbn:"978-1-78923-533-3",printIsbn:"978-1-78923-532-6",pdfIsbn:"978-1-83881-537-0",doi:"10.5772/intechopen.71213",price:119,priceEur:129,priceUsd:155,slug:"evolving-strategies-in-peritoneal-dialysis",numberOfPages:114,isOpenForSubmission:!1,isInWos:null,hash:"76bb5dc2ce63f0026f7993b54f062861",bookSignature:"Edward T. 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He trained at the University of\nCalifornia at Los Angeles (UCLA) from 1973 to 1978. His faculty\npositions include UCLA, University of Utah, Medical College of\nVirginia, and University of South Dakota. Other positions include professor and chairman emeritus, Department of Internal\nMedicine, University of South Dakota, Sanford School of Medicine; and Bush Foundation of Minnesota Sabbatical Fellowship in Critical Care, Department of Anesthesiology at the University of Iowa in 2009. Dr. Zawada Jr. is board certified by the\nAmerican Board of Internal Medicine in Internal Medicine, Nephrology, Geriatrics, and Critical Care Medicine. Other board certifications include Nutrition and\nClinical Pharmacology. He is a Master of the American College of Physicians and\nFellow of the American College of Critical Care Medicine, the American Society of\nNephrology, the American Society of Hypertension, the American College of Chest\nPhysicians, the American College of Clinical Pharmacology, the American College\nof Nutrition, and the American Heart Association.",institutionString:"University of South Dakota",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"8",totalChapterViews:"0",totalEditedBooks:"5",institution:{name:"University of South Dakota",institutionURL:null,country:{name:"United States of America"}}}],equalEditorOne:null,equalEditorTwo:null,equalEditorThree:null,coeditorOne:null,coeditorTwo:null,coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"1163",title:"Nephrology",slug:"nephrology"}],chapters:[{id:"60480",title:"Introductory Chapter: Peritoneal Dialysis, Overview and Current Concepts",doi:"10.5772/intechopen.75627",slug:"introductory-chapter-peritoneal-dialysis-overview-and-current-concepts",totalDownloads:356,totalCrossrefCites:0,totalDimensionsCites:0,signatures:"Edward T. 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\r\n\tCysticercosis, caused by the metacestode stage of Taenia solium, is a serious health and veterinary problem in many developing countries and is considered one of the most important neglected tropical diseases in developed countries. In humans, T. solium cysticerci cause neurocysticercosis, which affects ~50 million people worldwide, and it has been considered as an emergent disease in the United States. T. solium also infects pigs, its intermediate host, leading to major economic losses.
\r\n\r\n\tWhen humans ingest undercooked contaminated pork meat, the adult worm develops in the small intestine. After two months of asymptomatic infection, this tapeworm starts producing thousands of eggs, that, once released with the stools, can contaminate the environment, infecting pigs (rapidly differentiating into cysticerci mainly in the muscle) and humans (where most severe symptoms are observed due to the presence of cysticerci in the brain). Thus, maintenance of the parasite's life cycle depends on the adult tapeworm development. Even in communities which do not rear or consume pigs, human neurocysticercosis can be found, because of the presence of a tapeworm carrier. Furthermore, tapeworm development in turn depends on scolex evagination, the initial step through which a single cysticercus becomes an adult parasite with the capability of producing infective eggs. A great deal of scientific advances on the field has been producing in recent times, all on the most important fields of the disease: vaccination, epidemiology, current drug design, diagnostic and host-parasite interaction at all levels. However, to date, there is no actualized book dealing with the recent advances in such an important disease in the world.
\r\n\r\n\tThis book will intend to provide the reader with a comprehensive overview of the current state-of-the-art in cysticercosis featuring an easy-to-follow, vignette-based format that focuses on the most important evidence-based developments in this critically important area.
",isbn:"978-1-83969-395-3",printIsbn:"978-1-83969-394-6",pdfIsbn:"978-1-83969-396-0",doi:null,price:0,priceEur:0,priceUsd:0,slug:null,numberOfPages:0,isOpenForSubmission:!1,hash:"16dae70f4745a1873fbeb34e67007b24",bookSignature:"Prof. Jorge Morales-Montor, Dr. Abraham Landa and Dr. Luis Terrazas",publishedDate:null,coverURL:"https://cdn.intechopen.com/books/images_new/10354.jpg",keywords:"Delivering Methods, DNA Vaccines, Diagnostic of Cysticercosis, Diagnostic of Taeniosis, Epidemiology of Cysticercosis, Epidemiology of Neurocysticercosis, New Drugs Available, Drug-Design, Taenia Solium, Clinical Trials, Taenia Crassiceps, Immune Response",numberOfDownloads:null,numberOfWosCitations:0,numberOfCrossrefCitations:null,numberOfDimensionsCitations:null,numberOfTotalCitations:null,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"November 23rd 2020",dateEndSecondStepPublish:"December 21st 2020",dateEndThirdStepPublish:"February 19th 2021",dateEndFourthStepPublish:"May 10th 2021",dateEndFifthStepPublish:"July 9th 2021",remainingDaysToSecondStep:"2 months",secondStepPassed:!0,currentStepOfPublishingProcess:4,editedByType:null,kuFlag:!1,biosketch:"A pioneering researcher in Neuroinmunoendocrinology of several parasite infections, including cysticercosis. He has published over 153 papers, has edited 12 books, and written around 50 book chapters. Head of the Laboratory of Neuroimmunoendocrinology, Institute of Biomedical Research in UNAM, Mèxico.",coeditorOneBiosketch:"A pioneering researcher in molecular parasitology of Taenia solium cysticerci. He was part of the team that sequenced the Taenia solium genome. He has published over 33 papers on cysticercosis. Head of the Laboratory of Molecular Parasitology in UNAM, Mèxico.",coeditorTwoBiosketch:"A pioneering researcher in studying the immunology of taeniasis/cysticercosis, appointed Head of the Unit of Experimental Biomedicine. Recently appointed as Director of the Office of Development and Cultural and Scientific Relationships in the School of Superior Studies Iztacala, UNAM.",coeditorThreeBiosketch:null,coeditorFourBiosketch:null,coeditorFiveBiosketch:null,editors:[{id:"63810",title:"Prof.",name:"Jorge",middleName:null,surname:"Morales-Montor",slug:"jorge-morales-montor",fullName:"Jorge Morales-Montor",profilePictureURL:"https://mts.intechopen.com/storage/users/63810/images/system/63810.jpg",biography:"Dr. Jorge Morales-Montor studied biology at the Iztacala UNAM Faculty of Higher Studies, obtaining the title in 1992. He obtained a\ndoctor’s degree in October 1997. His doctoral thesis was recognized with the Lola and Igo Flisser-PUIS Award to the best graduate thesis at thenational level in theareaofparasitology,a recognition that he has also later received as a tutor, since one of his doctorate students won the same award in 2008. In November 1997, he began a postdoctoral stay at theDepartment of CellularBiology at the UniversityofGeorgia, USA, in the laboratory of Dr. Raymond T. Damia´n, one of the most recognized parasitologists in the world. Dr. Morales received a grant from the Fogarty Foundation (one of the most prestigious in Ibero-America) to carry out research on schistosomiasis in the baboon, being a Pan American Fellow for 4 years. Dr. Ray Damia´n would write years later, which assured that\nwithout a doubt, Jorge Morales-Montor had been the best postdoctoral researcher with whom he collaborated in his nearly 35-year career. He was repatriated to Mexico in 2001 by CONACYT and joined the Department of Immunology of the Institute of Biomedical\nResearch of UNAM as Associate Investigator “C”. In just 9 years, he managed to climb the entire ladder of university academic positions, to receive its tenure track positionas a Definitive C Titular Researcher at the Institute of Biomedical Research. The same is reflected in the Level of Premiums for Academic Performance, where it has reached the highest level currently: Level D, for the third\nconsecutive period. Also in the National System of Researchers, he has had the same growth, starting in 1997 as a candidate, and, to date, being promoted to Level III, the highest, for the third consecutive period. Dr.Morales-Montor has been invited to participate\nin different congresses (more than 100). In addition, he is part of the editorial committee of more than 15 indexed international\njournals, nd Editor in Chief of 3. Some of his most important contributions are partially determining the role of steroid hormones in immunological sexual dimorphism, in the polarization of the immune response, and in the antigenic presentation.He has alsomade very relevant studies in relation to how different physiological stages, how the estrous cycle, age, sex, or pregnancy affect the functioning of\nthe immune, endocrinological, and nervous system, and what molecules could be the determinants in this context of net. It has been\nshown that the central nervous system is involved in the regulation of the immune response to parasitic infections, and the effect\nof this activation on various behaviors of the infectedhost. But the centralnervous system has provided interesting data about its\nimpact in the parasitology approach. For instance, a modern concept is depicted by how the central nervous system modulates\nthe gene and proteomic regulation of the different sex steroids in parasites,which are involved in important functions of parasites\nsuch as establishment, growth, and reproduction. Finally, the practical use of the knowledge acquired by the earlier mentioned\nstudies has been applied to a theory that he calls old drugs, new uses: the use of hormones and antihormones as antiparasitic\ntherapy. He has also entered the study of environmental contamination, specifically endocrine disruptors and disease, studying\ntheir role in two very important diseases in the country: cancer and obesity, projects with which he has formed two consortiums\nof investigation. Its results are a very important contribution to the health of both Mexicans and Latin Americans in general, since\nthis is where serious health problems related to parasitic infections, cancer, and obesity are concentrated.His investigations are characterized by an exhaustive and meticulous experimental work, and his scientific production already has 153 articles in international indexed journals, and the majority as the first author or corresponding author. He hasmore than 3000 citations to his works, and an h-index of 29, one of the highest in the country’s scientific community. His articles published in high-impact international\njournals include Nature, PlosOne, Journal of Immunology, Journal of Infectious Diseases, Journal of Interferon and Cytokine Research,\nand among others. In fact, recently, his 2015 article, The Role of Cytokines in Breast Cancer Development and Progression, published in the Journal of Interferon and Cytokine Research, was the subject of a press release released by Mary Ann Liebert Publications. This is sent all over the world, to newspapers, Journals, scientists, radio, TV, popular magazines, to what is considered as a very important contribution in a certain area of science. Very few scientific articles are released as “press release.” He is also the 4th most cited author in the area of parasitology in the country. He has also edited several books and published more than 55 chapters in books, national and foreign. In this area, recently, the chapter “The Role of Sex Steroids in the Host-Parasite Interaction,” published in the international\nbook “Sex Steroids” in 2012, reached the figure of 68,000 downloads, which means the degree of attention that has after receiving\nhis work; the foregoing makes it clear that Dr. Morales-Montor’s work is highly relevant and widespread amongthenational and international academic community, and his brilliant career has earned him more than 30 awards, such as the Miguel Aleman Valdez Award in the area of Health 2006, the Distinction National University for Young Academics in the area of Research in Natural Sciences 2006, the CANIFARMA Veterinary Prize 2007 and 2009 the Heberto Castillo Martı´nez Capital City Award for Young Latin American Academics in Basic Research, and for the third consecutive congress, in 2011, one of his works was awarded the “Dr. Jose Eleuterio Gonza´lez” Award, for the best work of and research at the XXVI National Congress of Research in Medicine, to name just a few of its achievements. He has also mentored and graduated more thn 60 students at all levels (Baccularate, Masters and Doctorate) and also been awarded many distinctions, such as joining the Mexican Academy of Sciences (2005), and being one of the few Mexican scientists to be inducted to the Latin American Academy of Sciences (2008), The National Academy of Medicine, the New York Academy of Sciences, the American Association of Immunologists are deserved recognitions for his academic quality and career. His academic leadership is reflected in the trust and respect that his peers confer on him, having been President of the Mexican Society\nof Parasitology (one of the oldest and most prestigious scientific societies in the country) and currently being President, and founding member, of the Mexican Society of Neuroimmunoendocrinology, since 2011. Due to its scientific curiosity, it is in the process of founding the Mexican Society for Translational Environmental Biomedicine. He has been invited to edit special volumes\nin various magazines with international circulation and is a member of the editorial committee of magazines of\nimportance in his area of work, such as ParasiteImmunology, The OpenParasitologyJournal, among others. He has been a jury for\nthe Arturo Rosenblueth Awards for the best CINVESTAV Doctoral Thesis, a jury for the Lola and Igo Flisser-PUIS 2010 Awards, and\na jury for the Heberto Castillo Award, for the best Latin American Researcher 2012, awarded by the Federal District Government.\nIt is noteworthy that he is an outstanding scientist, who has contributed to the scientific research of Mexico with the generation of new frontier knowledge in the world and with the training of high-level human resources.",institutionString:"National Autonomous University of Mexico",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"3",totalChapterViews:"0",totalEditedBooks:"0",institution:{name:"National Autonomous University of Mexico",institutionURL:null,country:{name:"Mexico"}}}],coeditorOne:{id:"332210",title:"Dr.",name:"Abraham",middleName:null,surname:"Landa",slug:"abraham-landa",fullName:"Abraham Landa",profilePictureURL:"https://mts.intechopen.com/storage/users/no_image.jpg",biography:'He is a Master and Doctor of Science from UNAM, he did his post-doctorate at the Harvard University School of Public Health and his sabbatical at the Tufts University in Boston. He began his career as a teacher at the Faculty of Medicine UNAM in 1992, as an assistant in the subject of Biochemistry and Molecular biology to later be the owner of it. Is currently Full Professor "C" of T.C Definitive. It is Level “D” of the PRIDE and Level III of the National Research System. Academic-administrative positions: Representative of Postgraduate Tutors in Biological Sciences (2003-2006), in Biological Sciences (2003-2006), Member of the Review Commission of Nonconformities of the Personnel Performance Bonus Program Academic (PRIDE, 2002-2005), Secretary of the Mexican Society of Parasitology (2010-2011), Member of the Technical Council of the Faculty of Medicine (2006-2013) and currently a Member of the Judging Commission Research and Postgraduate Program CAABQyS of the FES-Iztacala (2015-1017).\r\nAwards and distinctions won the Scholarship awarded by the McArthur Foundation (1988-1989), Second place in the IV Parasitology Prize "Lola and Igo Flisser" 1992, the "Gabino Barreda" medal for his Doctorate in Science studies, 1997 and the medal "Nayarit for Scientific and Technological Research in 2001". Contributions and Scientific Productivity His research has been directed to the study of the molecular biology of Cestodes, especially of Taenia solium. He pioneered cloning and characterization of cestode genes and participated in the Consortium that carried out the university megaproject of the Taenia solium genome and three genomes\r\nmore than cestodes that resulted in a 2013 publication in the journal Nature. He has obtained with collaborators from the Institute of Chemistry, Faculty of Chemistry and from UAM the first crystal and inhibitor for a protein in cestodes (Cu / Zn superoxide dismutase), developed a recombinant antibody that inhibits triose phosphate isomerase. Has characterized the 3 glutathione transferases (24, 25, 26 kDa) that form the main system of detoxification and has contributed knowledge about the regulation of transcription, the foregoing has allowed reasonable knowledge of the cestodes and the diseases they cause. As a result of your work\r\nscientist has 58 publications, 12 book chapters, plus 2 books. Teaching and Training of Human Resources: Has taught since 1991, 30 courses and topics at the Postgraduate level. He has also directed 30 undergraduate theses, 9 Master\'s, 1 Specialization and 9 Doctorate. Almost all of his students PhD students are active researchers in Mexico and abroad. Doctor Landa is an active participant in conferences, as a member of committees tutorials, professional degree examinations in all programs of Postgraduate of the UNAM.',institutionString:"National Autonomous University of Mexico",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"0",totalChapterViews:"0",totalEditedBooks:"0",institution:{name:"National Autonomous University of Mexico",institutionURL:null,country:{name:"Mexico"}}},coeditorTwo:{id:"332215",title:"Dr.",name:"Luis",middleName:null,surname:"Terrazas",slug:"luis-terrazas",fullName:"Luis Terrazas",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0033Y000031RIzxQAG/Profile_Picture_1600754945533",biography:'He is a Master and Doctor of Science from UNAM, he did his post-doctorate at the Harvard University School of Public Health and his sabbatical at the Tufts University in Boston. He began his career as a teacher at the Faculty of Medicine UNAM in 1992, as an assistant in the subject of Biochemistry and Molecular biology to later be the owner of it. Is currently Full Professor "C" of T.C Definitive. It is Level “D” of the PRIDE and Level III of the National Research System. Academic-administrative positions: Representative of Postgraduate Tutors in Biological Sciences (2003-2006), in Biological Sciences (2003-2006), Member of the Review Commission of Nonconformities of the Personnel Performance Bonus Program Academic (PRIDE, 2002-2005), Secretary of the Mexican Society of Parasitology (2010-2011), Member of the Technical Council of the Faculty of Medicine (2006-2013) and currently a Member of the Judging Commission Research and Postgraduate Program CAABQyS of the FES-Iztacala (2015-1017).\r\nAwards and distinctions won the Scholarship awarded by the McArthur Foundation (1988-1989), Second place in the IV Parasitology Prize "Lola and Igo Flisser" 1992, the "Gabino Barreda" medal for his Doctorate in Science studies, 1997 and the medal "Nayarit for Scientific and Technological Research in 2001". Contributions and Scientific Productivity His research has been directed to the study of the molecular biology of Cestodes, especially of Taenia solium. He pioneered cloning and characterization of cestode genes and participated in the Consortium that carried out the university megaproject of the Taenia solium genome and three genomes\r\nmore than cestodes that resulted in a 2013 publication in the journal Nature. He has obtained with collaborators from the Institute of Chemistry, Faculty of Chemistry and from UAM the first crystal and inhibitor for a protein in cestodes (Cu / Zn superoxide dismutase), developed a recombinant antibody that inhibits triose phosphate isomerase. Has characterized the 3 glutathione transferases (24, 25, 26 kDa) that form the main system of detoxification and has contributed knowledge about the regulation of transcription, the foregoing has allowed reasonable knowledge of the cestodes and the diseases they cause. As a result of your work\r\nscientist has 58 publications, 12 book chapters, plus 2 books. Teaching and Training of Human Resources: Has taught since 1991, 30 courses and topics at the Postgraduate level. He has also directed 30 undergraduate theses, 9 Master\'s, 1 Specialization and 9 Doctorate. Almost all of his students PhD students are active researchers in Mexico and abroad. Doctor Landa is an active participant in conferences, as a member of committees tutorials, professional degree examinations in all programs of Postgraduate of the UNAM.',institutionString:"National Autonomous University of Mexico",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"0",totalChapterViews:"0",totalEditedBooks:"0",institution:{name:"National Autonomous University of Mexico",institutionURL:null,country:{name:"Mexico"}}},coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"16",title:"Medicine",slug:"medicine"}],chapters:null,productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"},personalPublishingAssistant:{id:"280415",firstName:"Josip",lastName:"Knapic",middleName:null,title:"Mr.",imageUrl:"https://mts.intechopen.com/storage/users/280415/images/8050_n.jpg",email:"josip@intechopen.com",biography:"As an Author Service Manager my responsibilities include monitoring and facilitating all publishing activities for authors and editors. 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Harvey and Nigel Gericke",authors:[{id:"60270",title:"Prof.",name:"Alan",middleName:null,surname:"Harvey",fullName:"Alan Harvey",slug:"alan-harvey"},{id:"107324",title:"Dr",name:"Nigel",middleName:"Peter",surname:"Gericke",fullName:"Nigel Gericke",slug:"nigel-gericke"}]},{id:"21541",title:"Morphological Disparity: An Attempt to Widen and to Formalize the Concept",slug:"morphological-disparity-an-attempt-to-widen-and-to-formalize-the-concept",totalDownloads:2468,totalCrossrefCites:0,signatures:"Igor Ya. Pavlinov",authors:[{id:"50006",title:"Dr.",name:"Igor",middleName:null,surname:"Pavlinov",fullName:"Igor Pavlinov",slug:"igor-pavlinov"}]}]},relatedBooks:[{type:"book",id:"2984",title:"The Species Problem",subtitle:"Ongoing Issues",isOpenForSubmission:!1,hash:"412f4d7e90c7760651420c3fa397f600",slug:"the-species-problem-ongoing-issues",bookSignature:"Igor Ya. Pavlinov",coverURL:"https://cdn.intechopen.com/books/images_new/2984.jpg",editedByType:"Edited by",editors:[{id:"50006",title:"Dr.",name:"Igor",surname:"Pavlinov",slug:"igor-pavlinov",fullName:"Igor Pavlinov"}],equalEditorOne:null,equalEditorTwo:null,equalEditorThree:null,productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"},chapters:[{id:"42174",title:"The Species Problem, Why Again?",slug:"the-species-problem-why-again-",signatures:"Igor Ya. Pavlinov",authors:[{id:"50006",title:"Dr.",name:"Igor",middleName:null,surname:"Pavlinov",fullName:"Igor Pavlinov",slug:"igor-pavlinov"}]},{id:"42175",title:"The Species Problem: A Conceptual Problem?",slug:"the-species-problem-a-conceptual-problem-",signatures:"Richard A. Richards",authors:[{id:"150948",title:"Prof.",name:"Richard",middleName:null,surname:"Richards",fullName:"Richard Richards",slug:"richard-richards"}]},{id:"42176",title:"Biological Species as a Form of Existence, the Higher Form",slug:"biological-species-as-a-form-of-existence-the-higher-form",signatures:"Victor Prokhorovich Shcherbakov",authors:[{id:"151276",title:"Dr.",name:"Victor",middleName:null,surname:"Shcherbakov",fullName:"Victor Shcherbakov",slug:"victor-shcherbakov"}]},{id:"41402",title:"Defining ‘Species,’ ‘Biodiversity,’ and ‘Conservation’ by Their Transitive Relation",slug:"defining-species-biodiversity-and-conservation-by-their-transitive-relation",signatures:"Kirk Fitzhugh",authors:[{id:"149620",title:"Dr.",name:"Kirk",middleName:null,surname:"Fitzhugh",fullName:"Kirk Fitzhugh",slug:"kirk-fitzhugh"}]},{id:"40674",title:"Transitioning Toward a Universal Species Concept for the Classification of all Organisms",slug:"transitioning-toward-a-universal-species-concept-for-the-classification-of-all-organisms",signatures:"James T. 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Mayden",authors:[{id:"148082",title:"Prof.",name:"Richard",middleName:null,surname:"Mayden",fullName:"Richard Mayden",slug:"richard-mayden"}]},{id:"42188",title:"Conspecific Recognition Systems and the Rehabilitation of the Biological Species Concept in Ornithology",slug:"conspecific-recognition-systems-and-the-rehabilitation-of-the-biological-species-concept-in-ornithol",signatures:"V. S. Friedmann",authors:[{id:"152904",title:"Dr.",name:"Friedmann",middleName:null,surname:"Vladimir",fullName:"Friedmann Vladimir",slug:"friedmann-vladimir"}]},{id:"42504",title:"Species Delimitation: A Decade After the Renaissance",slug:"species-delimitation-a-decade-after-the-renaissance",signatures:"Arley Camargo and Jack Jr. Sites",authors:[{id:"150554",title:"Dr.",name:"Jack W.",middleName:null,surname:"Sites, Jr.",fullName:"Jack W. Sites, Jr.",slug:"jack-w.-sites-jr."}]},{id:"42194",title:"Darwin’s Species Concept Revisited",slug:"darwin-s-species-concept-revisited",signatures:"David N. Stamos",authors:[{id:"151283",title:"Dr.",name:"David",middleName:"N.",surname:"Stamos",fullName:"David Stamos",slug:"david-stamos"}]}]}]},onlineFirst:{chapter:{type:"chapter",id:"65506",title:"Endoplasmic Reticulum-Associated Degradation (ERAD)",doi:"10.5772/intechopen.82043",slug:"endoplasmic-reticulum-associated-degradation-erad-",body:'The endoplasmic reticulum (ER) is an extensive network of flattened, membrane-enclosed tubes or sacs that extends throughout the cytosol [1]. ER has important roles in many biochemical processes required for cell survival and normal cellular functions. ER regulates these cellular processes through proteins that are localized in its complex network structures [1, 2, 3]. In addition to protein synthesis, significant cellular activities such as protein transport and folding, lipid and steroid synthesis, carbohydrate metabolism, calcium storage and protein quality control processes occur in the ER [1, 2, 3, 4].
Approximately one-third of all newly synthesized proteins are targeted to the ER and traffic to other organelles of secretory pathway, plasma membrane or the extracellular space [5]. Protein translocation to the ER occurs through Sec61 complex [6, 7]. As synchronized with translocation, protein is exposed to the ER’s oxidizing and calcium-rich environment, which is suitable for protein folding and co- and post-translational modifications such as glycosylation, disulfide bond formation and glycosylphosphatidylinositol (GPI) anchoring [8]. During this folding process, many proteins such as lectin-type molecular chaperones (e.g., calnexin (CNX) or calreticulin (CLR)), HSP70-like chaperone BiP) and enzymes like protein disulfide isomerases (PDI) work in association with each other [4, 9, 10]. Conformational maturation and folding of the proteins in the ER are instantly controlled through the added N-glycan groups to decide whether the proteins are directed to distant compartments via the secretory pathway or included in the refolding cycle [11, 12].
The folding process is not completely accurate. In mammals, 30% of all newly synthesized proteins are estimated to be incorrectly folded [13]. However, genetic mutations, errors in transcription and translation, toxic compounds and cellular stresses such as defects in cellular redox regulation due to hypoxia, oxidants and reducing agents that interact with disulfide bonds in the ER lumen, glucose starvation and abnormalities in calcium regulation lead to a significant increase in the ratio of incorrectly folded proteins [4, 11, 14]. Adequate removal of these unwanted proteins is crucial for protecting cells from proteotoxicity caused by the formation of protein aggregates through the re-opening of hydrophobic residues as well as by unfolded or misfolded proteins that may compete with their properly folded counterparts for substrate binding or for complex formation with partners. Even though the primary damage of these unwanted proteins is restricted to the cell they reside, the damage gets wider if it is a secretory protein [11]. Therefore, there is a robust control via “Protein Quality Control Mechanisms” for the removal of defective proteins in living cells, and thus, only properly folded proteins are allowed to exit from ER lumen to the secretory pathway [11, 15, 16, 17, 18]. When the folding process fails, the terminal mannose residues from the core glycan chain are gradually removed, allowing the proteins to be recognized by mannose-specific lectins and defective proteins are transferred to the 26S proteasome for degradation through the protein quality control mechanism called “ER-associated degradation (ERAD)” [19, 20, 21].
In addition to misfolding proteins, ERAD also targets some proteins that might fold into their native structures under the right conditions and also orphan subunits of oligomeric complexes. The chloride channel protein CFTR (cystic fibrosis transmembrane conductance regulator) is the best example, where it is targeted to ERAD as a consequence of its complex and inefficient folding pathway. The low folding efficiency is further decreased upon mutation as seen in CFTR∆F508. CFTR∆F508 is the most common mutation found in cystic fibrosis patients, can fold and function in plasma membrane; thus, degradation of CFTR via ERAD is obtrusive. ERAD also functions in supporting the correct stoichiometry of multimeric protein complexes by degrading components that are produced in excess of the limiting monomer [22]. For example, the unassembled subunits of T cell receptor-like TCRα and CD3δ are also well-known ERAD substrates [23]. These proteins contain charged residues in the intramembrane sections promoting the assembly of complexes. However, when oligomerization is not proper, these residues might initiate degradation via recruiting specific ERAD factors [23].
ERAD also functions in cell homeostasis by regulating the endogenous levels of many enzymes and signal molecules especially those localized to the ER membrane or plasma membrane under physiological conditions [24]. For instance, ERAD plays a homeostatic role in the regulation of HMG-CoA reductase (HMGR), which is the key enzyme of cholesterol metabolism; apolipoprotein B, an essential secreted protein member of triacylglycerol-rich lipoproteins responsible for the export of lipids, triglycerides and cholesterol; hepatic cytochrome P450 enzyme 3A4 metabolizing endo- and xenobiotics; IP3 receptor, an ER-localized protein allowing Ca2+ release by binding seconder messenger inositol 1,4,5-triphosphate (IP3); type II iodothyronine deiodinase, an ER-localized enzyme converting thyroxin (T4) to the biologically active hormone triiodothyronine (T3) and GABA neurotransmitter receptor responsible for the reduction of neuronal excitability and the tumor metastasis suppressor KAI1 levels [22, 25, 26, 27, 28].
Some viruses hijack the ERAD system through encoding effectors by serving as adaptors that redirect correctly folded molecules towards degradation. US2 and US11, the human cytomegalovirus gene products, induce degradation of major histocompatibility complex (MHC) class I heavy chain, which enables virus-infected cell to avoid detection by the immune system [29]. Similarly, Vpu is a glycoprotein encoded in the human immunodeficiency virus (HIV-1) genome and binds and targets newly synthesized CD4 for degradation [30], allowing them to evade immunosurveillance. Moreover, toxins like diphtheria, cholera and ricin enter the cell by endocytosis and move to the ER. They use the ERAD system to escape from the ER lumen and gain access to their enzymatic substrates in the cytoplasm [31].
ERAD is a highly complicated and regulated mechanism in which the diversity and combination of components change according to the protein to be destroyed [19, 20, 21, 32]. Maturation-defective proteins are removed from the ER lumen or lipid bilayer by retrotranslocation through the ERAD pathway and degraded by proteasome. The ubiquitin system is an integral part of the ERAD and is composed of factors necessary for the recruitment, processing and binding of ubiquitin chains to substrates [24]. In other words, ERAD is composed of steps that include substrate selection, modification with ubiquitin chain, retrotranslocation and 26S proteasomal degradation. Several key molecules such as E1, E2, and E3 enzymes responsible for ubiquitin transfer, channel components responsible for retrotranslocation, chaperones and cofactor proteins function in a synchronized manner during ERAD pathway [12, 19, 20, 21].
This critical role of ERAD in the regulation of cell homeostasis is an evident that ERAD disorders will have important effects on cell survival. Furthermore, it has been shown that aberrations in ERAD function play a role in the pathology of nearly 70 diseases such as cystic fibrosis, α1-antitrypsin (AAT) insufficiency, diabetes, neurodegenerative diseases (Parkinson, Alzheimer\'s and Huntington\'s diseases), viral infection and albinism [4, 33].
In this section, the knowledge related to the basic mechanism and regulation patterns of the ERAD will be summarized and presented.
About 30% of the total proteins and all transmembrane proteins of the cell are synthesized in the ER, which acts as a portal for entry into the secretory pathway via the Sec61 channel [7, 8]. As being translocated, the N terminal hydrophobic signal sequence of newly synthesized protein is cleaved by a peptidase complex [34]. Co- and post-translational modifications such as disulfide bond formation, initial steps of N-glycosylation, and glycophosphatidylinositol (GPI) anchorage take place in the ER.
The oxidizing environment of ER assists the formation of disulfide bonds, which stabilizes tertiary protein structure and facilitates protein assembly. During the folding process, disulfide bonds are formed through the oxidation of pairs of free thiols on cysteine residues by protein disulfide isomerases (PDIs). PDIs act as cycles, and after initial oxidation, disulfide bonds are sometimes isomerized by PDI and ERp57, which is a thiol oxidoreductase, in order to stabilize the correct folding of protein [35]. Conversely, the reduction of disulfide bonds of misfolded proteins is necessary for retrotranslocation step of ERAD. Indeed, PDI enables the retrotranslocation of the simian virüs-40 (SV-40) and cholera toxin [36, 37]. ERdj5, an ER oxidoreductase, reduces disulfide bonds and interacts with EDEM (ER-degradation enhancing mannosidase-like protein) and also accelerates the step of retrotranslocation of SV-40 [37]. ERDJ5 also regulates the degradation of disease-causing α1-antitrypsin variant (null Hong Kong) [38].
Folding is aided by molecular chaperones shepherding against misfolding and unfolding. Chaperone-like glycans bind to N-glycans playing a crucial role in protein folding and degradation. It is apparent that N-glycosylation, quality control of protein folding and ERAD are functionally linked. After entering to the ER, a large majority of the newly synthesized polypeptide chain are being N-linked glycosylated. The oligosaccharyltransferase enzyme recognizes the Asn-X-Ser/Thr consensus sequence in the most of the nascent protein molecule and covalently integrates a high mannose containing core glycan groups (Glc3Man9GlcNAc2) from dolichol localized on the ER membrane to the protein [39]. Due to the very short half-life of triglycosylated form of protein-bound oligosaccharide, glycan processing starts immediately after the transfer of precursor glycan groups through glucosidase enzymes. Following cleavage of two of three glucose residues, the nascent protein could interact with quality control lectins like CNX and CLR. This interaction is preserved until cleavage of remaining glucose residue. After releasing the glycoprotein from CNX/CLR cycle, final glucose is also trimmed creating unglycosylated substrate. This compromises the interaction of substrate with the lectin chaperones. At this stage, if protein is properly folded, it could exit the ER for their final destination. However, if glycoprotein is still unfolded, it is retained in the ER and reglucosylated by UDP-glucose:glycoprotein glucosyltransferase and rebound with CNX and CLR giving protein more time for proper folding [40, 41]. It is not yet understood the mechanisms involved in the termination of reglycosylation/deglycosylation cycles. However, it is clear that, if the polypeptide chain cannot reach its mature form after repeated folding attempts, terminal mannose residues from the core glycan chain are gradually removed by ER α1,2-mannosidase I (ERMan1). ERMan1 produces Man8GlcNAc2 isomer by removing a mannose residue from the middle branch of N-glycans. By this trimming, glycoprotein becomes poorer substrates for reglycosylation and exit from the CNX cycle [11].
The hydrophobic patches of properly folded proteins are usually buried within the interior of soluble proteins. However, those patches could be exposed in misfolded proteins. If a protein has exposed hydrophobic surfaces, BiP binds to it in order to hide these aggregation-prone surfaces for proper folding attempts by preventing aggregation. However, if folding does not succeed or delayed, extended chaperone-misfolding protein interaction serve for a sophisticated process where protein is transferred to other chaperones and/or to the ERAD process [27, 42].
It is well accepted that the first step of ERAD is selection of misfolded proteins by chaperones. As early as 1999, it was found that yeast ERAD substrates strikingly differed in their requirement for the ER-luminal Hsp70, BiP [43]. The degradation of soluble substrates such as pαF and a mutant form of the vacuolar protease carboxypeptidase Y* (CPY*) were dependent on BiP, while degradation of transmembrane proteins Pdr5*p, Ste6-166p, Sec61-2p and Hmg2p occurred in a BiP-independent manner. In 2004, it has been shown that substrates with cytosolic domain such as Ste6-166p were degraded BiP-independently, while proteins with luminal defects required BiP, suggesting that depending on the topology of misfolded lesion (ER lumen, ER membrane and cytoplasm) cytosolic or luminal chaperones function in the recognition and targeting for the degradation [44].
It is possible to study substrate recognition during ERAD using model misfolded proteins. It is clear that de-mannosylation is required for degradation of misfolded glycoproteins since inhibition of this mannose trimming stabilizes misfolded glycoproteins in the ER [45]. Overexpression of ERMan1 accelerates the degradation of N-glycosylated proteins [39, 46]. The resulting Man8-GlcNAc2 containing glycoprotein after this trimming becomes a substrate for EDEM1 (ER-degradation enhancing mannosidase-like protein 1, Htm1p in yeast)—a mannosidase-related lectin in the ER. It was further proposed that misfolded glycoproteins interact with ERManI and EDEM1 for their ERAD, and lectin-carbohydrate interaction found to be crucial for EDEM substrate recognition [47]. Although ERMan1 was suggested to be a biological timer initiating the ERAD of misfolded proteins [48], recent studies revealed that mannosidases are not solely responsible for intensive demannosylation during ERAD, especially under non-basal conditions. Under ER stress (unfolded protein response active) conditions, the transcriptional elevation of EDEM1 enhances the ERAD efficiency by suppressing proteolytic downregulation of ERMan1 [49]. It appeared that EDEMs also play an important role in demannosylation of substrates [50]. EDEM1 also prevents reglycosylation and promotes retrotranslocation and degradation of some ERAD substrates [51]. On the other hand, while mannosidase homology domain (MHD) of Htm1p is necessary for substrate binding, mammalian EDEM1 binds misfolded proteins independent of MHD domain, and therefore, EDEM1 substrate binding may not require mannose trimming or even glycosylation [52]. Thus, in addition to N-linked oligosaccharide moieties of glycoproteins, EDEM1 can recognize the folding lesions of misfolded proteins. In summary, EDEMs are directly or indirectly involved in demannosylation of glycoproteins and/or serve as receptors that bind and target mannose-trimmed proteins for ERAD (Figure 1).
Protein quality control and targeting misfolding proteins to the ERAD.
Truncation of terminal mannose from branch C exposes α terminal α1,6-bonded mannose residues functioning as a recognition signal for ERAD lectins such as OS9 (Yos9 in yeast) and XTP3-B (Figure 2). Through their mannose-6-phosphate receptor homology (MRH) domain, both proteins primarily recognize α1,6-linked mannose j. Additionally, OS-9 also recognizes α1,6-linked mannose e and c [53].
Schematic representation of ERAD using the Hrd1 complex as model.
Several reports suggest that factors (EDEMs, OS9 and XTP3-B) required for substrate recognition and targeting reside within supramolecular complexes and/or interact with important ERAD regulators [54]. For example, EDEM1 interacts with CNX, receives substrates from CNX cycle and facilitates ERAD substrate degradation such as NHK-α1-antitrypsin mutant [55, 56, 57]. EDEM1 also associates with the components of ER retrotranslocation machinery. It is suggested that EDEM1 binds misfolded proteins and uses its MHD domain to target aberrant proteins to the ER-resident glycoprotein SEL1L protein of the Hrd1-SEL1L ubiquitin ligase complex [58]. SEL1L scaffolds several luminal substrate recognition factors and links them to Hrd1. OS9 and XTP3-B also associate with Hrd1-SEL1L complex, which also includes BiP and GRP94 [59, 60]. Furthermore, XTP3-B is proposed to link BiP with Hrd1 complex [60]. According to a hypothesis, these three chaperones (EDEM1, OS9 and XTP3-B) function as oligomers, where one monomer interacts with substrate and another with Hrd1-SEL1L complex [61]. Additionally, EDEM1 also interacts with Derlins, a transmembrane protein, which is a candidate for translocon [62]; furthermore, Derlin2 is shown to enhance the interaction of EDEM1 with a cytosolic AAA-ATPase p97, which couples ATP hydrolysis to the retrotranslocation of misfolded proteins [50].
It is clear that substrate recognition step of ERAD is a complicated mechanism, in which several different enzymes and chaperones having distinct but concerted roles in the ERAD are involved. Moreover, depending on substrates, the number and features of involved proteins vary. For example, concerted roles of EDEM, ERdj5 and BiP in the degradation of misfolded proteins have been suggested [63]. After exiting CNX-CLR cycle, EDEM1 further trims the Man8-GlcNAc2 glycan structure and ERdj5 reduces disulfate bonds. Concomitantly, ERdj5 activates BiP’s ATPase activity. ADP-bound BiP binds to the misfolded protein and holds it in a retrotranslocation component form until it transfers to the retrotranslocation complex [63].
ERAD is also involved in the quality control of non-glycosylated proteins, which is independent of lectin-like proteins. Immunoglobulin light chain (Ig-K-LC), a non-glycosylated ERAD substrate, is degraded in a BiP-dependent manner. Okuda-Shimizu and Hendershot have characterized an ERAD pathway for this non-glycosylated BiP substrate [64] and different protein interaction dynamics seen to play a role in this process. Ig-K-LC has two intramolecular disulfide bonds, and its fully oxidized form does not have ability to pass from the ER to the cytoplasm. BiP interacts with only partially oxidized form of the Ig, preventing the full oxidation of Ig-K-LC and thereby facilitating its release from the ER [64]. Furthermore, a transmembrane UBL domain-containing protein, homoCys-responsive ER-resident protein (HERP), has been implicated as a receptor for non-glycosylated BiP substrates [64]. HERP interacts with Derlin1, and the partially oxidized Ig-K-LC is transferred from BiP to the HERP-Derlin1-Hrd1 complex and subsequently directed to proteasomal degradation [65]. Besides BiP, ERdj5 as disulfide reductase is also indicated to be important for ERAD of non-glycosylated proteins [63]. The non-glycosylated substrates captured by BiP are transferred to ERdj5 for the cleavage of disulfide bonds. Then, these substrates are transferred to SEL1L by the help of BiP for retrotranslocation [63]. Besides BiP, both OS9 and XTP3-B have been implicated in the ERAD of non-glycosylated proteins [12].
Ubiquitin is a 76 amino acid polypeptide encoded on multiple genes. It is ubiquitously expressed in all eukaryotic cells and highly conserved from yeast to human. Ubiquitin can be covalently conjugated to other proteins as monomers or as chains through a complex, highly regulated process called ubiquitination. Although there are reports for evidence of Ser- and Thr-linked ubiquitination, ubiquitin chain is generally attached on the Lys residue on misfolded protein. Lys-6, -11, -27, -29, 33, -48 and -63 are the residues used for ubiquitin linkage. Both the type of ubiquitination (mono/poly) and the linkages of ubiquitin chains affect the fate, localization, stability and activity of target proteins [9].
Ubiquitination has a regulatory role in almost all cellular processes by altering the fate and function of the proteins. The most well-established role of ubiquitination is targeting proteins for degradation by the 26S proteasome, and the most efficient way of targeting proteins to the proteasome is by tagging them with chains of ubiquitin [66]. This targeting requires modification of proteins with chains of four or more ubiquitins attached through lysine 48 (K48) and the specific recognition of these chains by the 19S cap of the 26S proteasome [67]. Mainly Lys-48 but rarely Lys-11-based polyubiquitin chains are reported to bind onto ERAD substrates [68].
Ubiquitination regulates several critical cellular functions, often by mediating the selective degradation of important regulatory proteins. Antigen presentation, inflammatory response induction and cell cycle progression are few examples. As expected, malfunctioning of ubiquitin-dependent proteolysis has implications for cancer and several inherited diseases, such as Angelman syndrome, Parkinson’s disease and Alzheimer’s disease [69].
The role of ubiquitination, however, is not limited to proteasomal targeting. The type of residue that the chain is built is critical for the fate of the ubiquitinated protein. Monoubiquitination has effects in protein trafficking, including endocytosis and lysosomal targeting. Polyubiquitin chains conjugated through K48 or other lysines (often K63) also have effect on proteasome-independent mechanisms, such as DNA repair, regulation of transcription factor activity and protein kinase activation [70].
Ubiquitination is a multi-enzyme process. Three enzymes are involved: E1-ubiquitin activating enzyme, E2-ubiquitin conjugating enzyme and E3-ubiquitin ligase. During ubiquitination, E1 forms a thiol-ester bond between its active cysteine and C-terminal glycine of ubiquitin in an adenosine triphosphate (ATP)-dependent manner. Ubiquitin on E1 is now activated and transferred to the active cysteine of E2 by a trans-thiolation reaction. E3 binds both to E2 and substrate and facilitates the formation of an isopeptide linkage between C-terminal glycine of ubiquitin and an internal lysine residue on substrate. Ubiquitin modification is dynamic and could be removed by deubiquitination enzymes (DUBs).
Today only 2 E1 enzymes and 35 E2 enzymes have been identified in mammals, but there are approximately 100 E3 in yeast and at least 600 in humans [71, 72]. E3s catalyzing the transfer of active ubiquitin moieties on the substrate are responsible for substrate specificity. There are two large families of E3s: (1) HECT [homologous to E6-associated protein (E6AP) C-terminus] domain E3s and (2) RING [really interesting new gene] domain E3s. HECT domain E3s share a 350-residue region harboring a strictly conserved cysteine residue that forms an essential thiol-ester intermediate during catalysis. That is why ubiquitin is transferred to the active-site cysteine of the HECT domain followed by transfer to substrate or to a substrate-bound multi-ubiquitin chain. The RING finger defines the largest family of E3s. RING fingers range from 40 to 100 amino acids and are defined by eight conserved cysteine and histidine residues that coordinate two zinc ions stabilizing a characteristic cross-braced conformation. For RING E3s, current evidence indicates that ubiquitin is transferred directly from E2 to substrate [69, 70].
Ubiquitination step marks ERAD substrates for proteasomal degradation. In yeast, Doa10p and Hrd1p ligases are mainly responsible for ubiquitination of ERAD substrates, but additional E3s shown to contribute to the ERAD under special circumstances [9]. Depending on the topology of misfolded lesion, factors required for ERAD vary. In yeast, three ERAD pathways have been proposed. ERAD-C, ERAD-L and ERAD-M target proteins with lesions in the cytoplasmic, luminal and membrane domains, respectively [44, 73, 74]. ERAD-L substrates use the Hrd1p ubiquitin ligase complex containing Hrd1p, Hrd3p, Usa1p, Der1p, and Yos9p, whereas ERAD-M substrates use Hrd1p and Hrd3p, only in some cases Usa1p [68]. Hrd3p is specifically important for structural integrity of Hrd1p complex. Hrd3p stabilizes Hrd1p, and when it is absent, Hrd1p is auto-ubiquitinated and rapidly degraded. Hrd3p and its mammalian homolog SEL1L also function as an adaptor bridging substrate recognition, ubiquitination and retrotranslocation in Hrd1-mediated ERAD. On the other hand, ERAD-C substrates interact with the Doa10p ubiquitin ligase complex. These three pathways have been identified only in yeast and mammalian has more complicated machinery. Even in yeast, some membrane proteins require both Doa10p and Hrd1p E3s; thus, these pathways could overlap [42].
Although Hrd1p and Doa10p are conserved evolutionary (mammalian homologs: Hrd1 and TEB4, respectively), the number of ERAD E3s in mammals is highly expanded. Besides Hrd1 and TEB4, gp78, RNF5/RMA1, RNF170, RNF185, Trc8, RNF103, RFP2, Fbx2, Fbx6, Parkin, CHIP and UBE4a are other characterized ERAD E3s [9, 27]. Hrd1 and gp78, both homologues to yeast Hrd1p, are the most studied ERAD E3 indicated for degradation of several substrates, some of which are associated with the quality of disease-related proteins. HMG-CoA reductase, apolipoprotein B, cytochrome P450 CYP3A4, CFTRΔF508, z-variant antitrypsin, CD3δ and KAI1 are shown to be degraded via gp78-mediated ERAD, whereas studies have been suggested that Hrd1 is important for the ERAD of GABAb receptor, Nrf2, Pael-receptor mutant tyrosinase, z-variant antitrypsin and gp78 [22, 75, 76, 77, 78]. Only a couple of substrates are known for other E3 ligases. It is also interesting that multiple E3s often function in the degradation on same substrate either in parallel or in tandem.
As Hrd1p in yeast, Hrd1 in mammals functions in a multi-protein complex. While it is complex with EDEM1, Derlins, OS9, XTP-3B and SEL1-L have been linked with degradation of glycosylated substrates (Figure 2), and another Hrd1 complex utilizing BiP, HERP and Derlin1 functions in the degradation of non-glycosylated substrates. Other ERAD factors have also been shown to interact with Hrd1 including UBXD2 and UBXD8 that interact with p97/VCP and recently identified chaperones such as ubiquilin and BAG6. Similarly, gp78, the second major mammalian ERAD E3 enzyme, functions in multiprotein complex in conjunction with E2 enzyme UBE2G2. Besides its diversity on substrate specificity, gp78 also has variety of different partners allowing its communication with proteins on both sites of ER membrane. gp78 uses a VIM (VCP-interacting motif) segment to bind p97/VCP [77] and CUE domain recruiting a multiprotein complex composed of Bag6 and its cofactors [79].
After initial E3-mediated ubiquitin attachment, ubiquitin chain extension (“polyubiquitination”) occurs by the covalent modification of additional ubiquitin monomers onto a Lys residue in a previously linked ubiquitin. This forms an extended isopeptide-linked polyubiquitin chain. In some selected cases, the cooperative extension of a polyubiquitin chain is by the E4s, ubiquitin chain extension enzymes, that facilitate ERAD [80, 81, 82].
The ERAD substrates must be retrotranslocated to the cytosol for proteasomal degradation and the cytoplasmic AAA+ ATPase p97 (VCP or Cdc48p in yeast) is the main retrotranslocation protein providing the mechanical force required for removal of proteins from the ER. It is an essential protein having many roles in diverse biological processes, such as endoplasmic reticulum-associated degradation (ERAD), homotypic membrane fusion, transcriptional control, cell cycle regulation, autophagy, endosomal sorting and regulating protein degradation at the outer mitochondrial membrane [83, 84, 85].
p97/VCP has a multidomain structure including N domain, D1 weak ATPase, D2 major ATPase and C domain [86, 87, 88]. p97/VCP functions as a homohexamer and D1 domain is responsible for oligomerization independent of nucleotide binding. The change in the conformation of hexameric ring by ATP hydrolysis is persistent with its function in retrotranslocation [88, 89].
The diversity in cellular functions of p97/VCP is dictated by the variety of its partner proteins that interact with its N domain. p97/VCP associates with several E3s like Hrd1 and gp78, DUBs like ataxin3 and YOD1 and ERAD accessory factors such as UbxD2 and VIMP. Moreover, many p97/VCP interacting proteins (Ufd1-Npl4 dimer, gp78 etc.) bind directly to ubiquitin. p97/VCP functions as a segregase using the energy from ATP hydrolysis to segregate ubiquitinated proteins from large immobile complexes of ER to the cytosol. This cytosolic protein is recruited to the ER membrane through its interaction with membrane-embedded ERAD components. There are at least seven different ERAD members that could interact with p97/VCP via certain motifs such as VIM motif (gp78 and SVIP), UBX domains (UBXD2 and UBXD8), SHP boxes (Derlin1 and Derlin2) and uncharacterized cytosolic regions of Hrd1 and VIMP that found to have p97/VCP-binding motif [12, 42, 90].
Retrotranslocation is tightly coupled with both ubiquitination and proteasomal degradation. In most cases, inhibiting ubiquitination prevents both degradation and retrotranslocation. The interaction of p97/VCP/CDC48p with its cofactor Ufd1-Npl4 dimer enhances its affinity to ubiquitin (Figure 2). However, it has been also suggested that Hrd1-mediated ERAD requires well-established retrotranslocation machinery, the p97/VCP–Ufd1–Npl4 complex, whereas the gp78 pathway needs only p97/VCP and Npl4 [75].
Many deubiquitinating enzymes (DUBs) in mammalian cells, including Ataxin3, USP13, USP25 and YOD1, are also implicated in the ERAD through physical interaction with ERAD core machinery [72, 91, 92]. Several studies revealed that p97/VCP interacts with DUBs. However, the function of DUBs in the ERAD is still not fully characterized. Otu1p (yeast homolog of YOD1) binds to CDC48p and trims the polyubiquitin chain, resulting oligoubiquitin chains with up to 10 ubiquitin molecules. It has been further suggested that releasing substrates from CDC48p requires DUBs [93]. Consistently, catalytically inactive YOD1 inhibits retrotranslocation of ERAD substrates [91]. In conclusion, many p97-associated DUBs serve as positive regulators of ERAD.
Several putative retrotranslocation channels have been proposed such as the Sec61 complex, members of Derlin family and polytopic E3s such as Hrd1 and gp78. Sec61 is one of the proposed channel protein mutants, which prevented degradation of some ERAD substrates in yeast [94, 95]. Cholera toxin also translocates from ER by utilizing Sec61 [96]. On the other hand, retrotranslocation of some other ERAD substrates has been suggested to depend on Derlins [97, 98], a family of polytopic transmembrane ER proteins linked to some ERAD substrates. Moreover, Derlin1 recruits p97/VCP [99], a key protein of retrotranslocation, which provides energy for the process. Derlin1 also interacts with some E3s like Hrd1, gp78 and RNF5 forming large complexes on the ER membrane [9]. Recently, Hrd1 ubiquitin ligase has been suggested to be the top candidate for retrotranslocation channel [9]. Auto-ubiquitination of Hrd1p in its RING finger domain triggers conformational change allowing the misfolded luminal domain of a substrate to move across the membrane. Thus, it was suggested that Hrd1 forms an ubiquitin-gated protein-conducting channel [33]. It has also been suggested that proteins might exit the ER via the formation of lipid droplets or lipid droplets serve as an intermediate step for substrates en route to the proteasome [100]. However, studies in yeast suggested that lipid droplet formation is dispensable for ERAD-L and ERAD-M [101].
Once retrotranslocated from ER to the cytosol, ERAD substrates should be rapidly targeted to the proteasome for degradation in order to avoid accumulation of aggregates in the cytosol. Consistently, proteasomal inhibition also stabilizes ERAD substrates in the ER lumen. For the coupling of retrotranslocation with degradation, ubiquitinated substrates must be recognized by cytosolic proteins functioning as ubiquitin receptors. Ubiquitin-binding domain containing proteins has ability to shuttle ubiquitinated proteins from retrotranslocation complex at the ER membrane to the proteasome since these proteins interact both with proteasome and p97/VCP. Indeed, it has been suggested that p97/VCP bridges the ER to the proteasome by forming a complex with mHR23B (homolog of yeast Rad23p)-PNGase [102] (Figure 2). In yeast, the substrates are probably transferred from CDC48p to the proteasome indirectly via ubiquitin- and proteasome-binding domains containing shuttling factors Rad23p and Dsk2p [103, 104]. Recently, Bag6/Bat3/Scythe has been characterized as a novel chaperone system with regulatory functions in protein degradation [79]. The chaperone holdase activity of this system keeps some retrotranslocated substrates in a soluble state for proteasome degradation. Bag6, also a partner protein of gp78 E3 enzyme, interacts with proteasome, and proteins like ubiquilin that known as proteasome adaptor proteins suggesting Bag6 might act between p97/VCP and proteasome to hand substrates off from retrotranslocation machinery to the proteasome.
Regulation of ERAD in normal and pathological conditions is also of great importance since hyper-ERAD may cause in loss-of-function phenotypes upon unnecessary degradation of folding intermediates as seen in CFTR and hypo-ERAD may result in gain-of-function phenotypes upon accumulation and/or aggregation of misfolded and unassembled proteins. Several studies suggested different regulation paths for ERAD activity via ubiquitin ligases and their dynamic ERAD complexes, UPR and endogenous ERAD inhibitors.
It is thought that ERAD functions at relatively low levels under basal conditions, but under proteotoxic stress its activity is enhanced. Accumulation of the unfolding or misfolding proteins in the ER lumen triggers “ER stress” by decreasing free chaperone levels [105]. In response to this cellular stress, the pathway known as the “Unfolded Protein Response (UPR)” is activated and results in specific cellular functions classified as adaptation, alarm and apoptosis [4]. Three transmembrane proteins with luminal domains that sense the changes in the ER environment function as UPR sensor proteins are inositol requiring enzyme-1 (IRE1), activating transcription factor 6 (ATF6) and protein kinase RNA-like endoplasmic reticulum kinase (PERK). PERK is a serine/threonine kinase, and IRE1 possesses both kinase and endoribonuclease domains [27, 50]. These sensors initiate signal transduction by sensing the presence of unfolded proteins in the ER lumen and thus control the UPR pathway [15, 18, 106]. All these transmembrane proteins interact with BIP under basal conditions. However, when unfolded proteins are present, BIP dissociates from the UPR sensor proteins. After dissociation of BIP, PERK and IRE1 dimerize and become activated by auto-phosphorylation, whereas ATF6 become translocated to the Golgi and proteolytically cleaved [27, 50]. Activated PERK phosphorylates translation factor eIF2α attenuating protein synthesis to limit protein load. IRE1 activates XBP-1 that enhances transcription of ERAD factors [27, 50]. On the other pathway, ATF6 upregulates many genes that encode ER-resident chaperones and folding assistants like BIP, CNX, CLR and PDI. To summarize, with the induction of UPR in the cell, the overall translation is inhibited for several hours primarily to slow down the entry of newly synthesized proteins to the ER, the amount of chaperones and ER protein folding capacity is increased for proper folding of accumulated unfolded proteins, and thus, the normal ER function and homeostasis are protected [4, 107]. UPR also enhances ERAD capacity by upregulating some of the ERAD genes to ensure that defective proteins are degraded when the folding attempts fail [21, 22, 23]. EDEM proteins, Hrd1, SVIP, OS9 and gp78, are only some of the targets of the ER stress-induced Ire1/Xbp1 pathway [62, 108, 109, 110, 111]. If the cellular stress is consistently increasing, UPR induces cell death mechanisms such as apoptosis or autophagy [4, 14, 112].
It has been suggested that large or prolonged variations such as change in Ca2+ or redox homeostasis, exposure to pathogens and large-scale accumulation of misfolded proteins may induce UPR to adapt ERAD activity. However, smaller or more transient fluctuations on ER load may be overcome rapidly by post-translational pathways that control stability, localization and assembly of ERAD components [23]. For example, reversible ADP ribosylation adapts BIP response for short-term fluctuations [113]. Reversible palmitoylation changes the sub-organelle distribution of CNX [114, 115]. Moreover, many ERAD factors/enhancers, including EDEM1, ER Man1, HERP, OS9, SEL1L and gp78, have fast turnover. This is important since when protein misfolding crisis is over, ERAD activity should rapidly turn back to the basal levels. Many ERAD factors then rapidly degraded via a process called ERAD tuning [23]. ERAD tuning does not require signal transduction from the ER to the nucleus [23]. Hrd1 was suggested to be a central regulator of ERAD tuning. It has been shown that Hrd1 ubiquitinates gp78 E3 enzyme and enhances its degradation, which in turn causes inhibition of gp78-mediated ERAD. Very recently, Hrd1 was also found to regulate the stability of OS9 [116]. Hrd1 also undergoes auto-ubiquitination to induce its own proteasomal degradation [117]. Another homeostatic control mechanism, in which ERAD activity itself is regulated post-translationally and independent of UPR, is degradation of EDEM1, OS9 and SEL1L by the E2 enzyme UBC6e, a component of Hrd1 supramolecular complex [118].
Another type of ERAD regulation occurs via substrate-specific adaptor, as reported for HMGR. The adaptor proteins, Insig1 or Insig2, bind to HMGR only in the presence of 24,25-dihydrolanosterol, an intermediate molecule in sterol biosynthesis. Under low sterol levels, HMGR is stable; however, when sterol levels are high, Insig-HMGR interaction become favored, leading delivery of HMGR to E3 complex following by its proteasomal degradation [119]. Likewise, ERAD-mediated degradations of apolipoprotein and IP3R are initiated when lipid levels are low and calcium levels are high, respectively [23].
DUBs are also proposed as factors that regulate ERAD. As explained above, several DUBs have been reported to interact with p97/VCP and function as positive regulators of retrotranslocation. Additionally, some DUBs are linked with the regulation of E3 enzyme stability. For example, USP19, an ER-anchored DUB, rescues HRD1 from proteasomal degradation and thereby regulates HRD1 stability [120]. Similarly, USP19 enhances the stability and activity of another E3 MARCH6 [121].
SVIP (small VCP interacting protein), a VCP-interaction motif (VIM) containing protein, is the first identified endogen ERAD inhibitor. SVIP interacts with p97/VCP and Derlin1 and inhibits the ubiquitination and degradation of gp78-dependent ERAD substrates [111]. Another endogen ERAD inhibitor is SAKS1. SAKS1 binds to the polyubiquitin chain of the substrate and p97/VCP and attenuates the ERAD process [122].
ERAD activity can also be controlled by hormonal regulation. Glucocorticoids have been suggested to ameliorate ER stress by promoting correct folding of secreted proteins and enhancing removal of misfolded proteins from the ER probably through induction of UPR. Recently, androgen-mediated regulation of ERAD has been reported. Androgen treatment upregulated the expression of Os9, p97/VCP, Ufd1, Npl4, Hrd1 and gp78, but downregulated ERAD inhibitor SVIP, which in turn enhanced the proteolytic activity of ERAD in androgen-sensitive prostate cancer cells [123]. Furthermore, the regulation of ERAD by androgen is mediated via AR and is partially or fully independent on the androgen-mediated induction of IRE1α branch [123].
The authors declare no conflict of interest.
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\n\nCorresponding authors will receive a 15% discount on their Open Access Publication Fees (OAPF) for Open Access book chapters or monograph publications. To use the discount you will need to verify your institutional email address. These discounts are valid from 2020 to 2022.
\n\nThe University of Massachusetts, Amherst is pledging funds via the Knowledge Unlatched program to ensure academics can publish Open Access content more easily.
\n\nCorresponding authors will receive a 10% discount on their Open Access Publication Fees (OAPF) for Open Access book chapters or monograph publications. To use the discount you will need to verify your institutional email address. These discounts are valid from 2020 to 2022.
\n\nThe University of Surrey is pledging funds via the Knowledge Unlatched program to ensure academics can publish Open Access content more easily.
\n\nCorresponding authors will receive a 10% discount on their Open Access Publication Fees (OAPF) for Open Access book chapters or monograph publications. To use the discount you will need to verify your institutional email address. These discounts are valid from 2020 to 2022.
\n\nMonographs Only
\n\n\n\nImportant: You must be a member or grantee of the above listed institutions in order to apply for their Open Access publication funds.
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