Open access peer-reviewed Edited Volume

Ubiquitin - Proteasome Pathway

Xianquan Zhan

Xiangya Hospital of Central South University

Covering

Ubiquitin E1 enzymes E2 enzymes E3 enzymes Substrate proteins Proteoasome Ubiquitination Ubiquitinomics Signaling networks Proteasome inhibitors Cancer Neurodegenerative diseases

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About the book

The ubiquitin-proteasome pathway (UPP) consists of ubiquitin, substate proteins, E1 enzymes, E2 enzymes, E3 enzymes, and proteasome. Ubiquitin is a highly conserved small proteins with 76 amino acids and about 8.5 kDa. E1 enzymes are ubiquitin-activating enzymes. E2 enzymes are ubiquitin-conjugating enzymes. E3 enzymes are ubiquitin ligases. The proteasome is a 26S protein complex, which contains one 20S core and two 19S lids. The UPP actually consists of a series of enzymatic reactions: E1 binds to ubiquitin in order to activate ubiquitin in ATP-dependent fashion, the activated ubiquitin is conjugated with E2, and then ubiquitin-conjugated E2 together with E3 ligases recognizes substrate proteins and covalently attaches ubiquitin (monomer or polyubiquitin chain) to substrate proteins (ubiquitinated proteins). Ubiquitinated proteins are then delivered to the proteasome for degradation into peptides or amino acids, which are further used for synthesis of new proteins. The mentioned substrate proteins include unneeded proteins and misfolded proteins within cells and tissues. Also, there are the deubiquitinating enzymes (DUB) that can remove the attached ubiquitin chain. Thus, ubiquitination / deubiquitination is a reversible processes. The UPP plays a crucial roles in degrading most of intracellular proteins and maintaining the balance between protein synthesis and degradation. Component changes in the UPP are associated with multiple pathophysiological processes, such as cancer and neurodengerative diseases. For example, mutated or overexpressed E3 ligases can act as oncogenes, while some E3 ligases and DUBs are also tumor suppressors. For example, the UPP is involved in synaptic function which regulates the nervous system. The UPP regulates multiple biological processes, including DNA repair, mitophagy, angiogenesis, RTK signaling, NF-kB signaling, and mitochondrial maintenance, which are dynamically regulated by ubiquitination. This book will focus on changes of UPP components, the methodology for studying UPP, protein ubiquitination, and applications of UPP in different diseases.

Publishing process

Book initiated and editor appointed

Date completed: October 29th 2019

Applications to edit the book are assessed and a suitable editor is selected, at which point the process begins.

Chapter proposals submitted and reviewed

Deadline for chapter proposals: November 19th 2019

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Deadline for full chapters: January 18th 2020

Once approved by the academic editor and publishing review team, chapters are written and submitted according to pre-agreed parameters

Full chapters peer reviewed

Review results due: April 7th 2020

Full chapter manuscripts are screened for plagiarism and undergo a Main Editor Peer Review. Results are sent to authors within 30 days of submission, with suggestions for rounds of revisions.

Book compiled, published and promoted

Expected publication date: June 6th 2020

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About the editor

Xianquan Zhan

Xiangya Hospital of Central South University

Professor Dr. Zhan received his undergraduate and graduate training in the fields of preventive medicine and epidemiology and statistics at the West China University of Medical Sciences in China from 1989 to 1999. He received his post-doctoral training in oncology and cancer proteomics for two years at the Cancer Research Institute of Human Medical University in China. In 2001, he went to University of Tennessee Health Science Center (UTHSC) in the USA, where he was a post-doctoral researcher and was focused on mass spectrometry and cancer proteomics. Then, in 2005 he was appointed as Assistant Professor of neurology at UTHSC. In 2006 he moved to Cleveland Clinic in the USA as a project scientist / staff, where he focused on studies of eye disease proteomics and biomarkers. He returned to UTHSC as Assistant Professor of neurology at the end of 2007, engaging in proteomics and biomarker studies of lung diseases and brain tumors, and initiating the studies of predictive, preventive, and personalized medicine (PPPM) in cancer. In 2010, he was promoted to Associate Professor of neurology, UTHSC. Currently, he is a Professor at Xiangya Hospital of Central South University in China, fellow of the Royal Society of Medicine (FRSM), the European EPMA National Representative in China, regular member of the American Association for the Advancement of Science (AAAS), European Cooperation of Science and Technology (e-COST) grant evaluator, Associate Editor of BMC Genomics, BMC Medical Genomics, EPMA Journal, and Frontiers in Endocrinology, and Executive Editor-in-Chief of Med One. He has published 118 peer-reviewed research articles, 16 book chapters, and 2 US patents. His current main research interests are focused on cancer proteomics and biomarkers studies, and the use of modern OMICS techniques and systems biology for PPPM in cancer, post-translational modifications, and on development and use of isotope-labeled 2DE-LC/MS for large-scale study of human proteoforms.

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Book chapters authored 4

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