The functional organization of eukaryotic cells requires the exchange of proteins, lipids, and polysaccharides between membrane compartments through transport intermediates. Small GTPases largely control membrane traffic, which is essential for the survival of all eukaryotes. Transport from one compartment of this pathway to another is mediated by vesicular carriers, which are formed by the controlled assembly of coat protein complexes (COPs) on donor organelles. The activation of small GTPases is essential for vesicle formation from a donor membrane. In eukaryotic cells, small GTP-binding proteins comprise the largest family of signaling proteins. The ADP-ribosylation factor 1 (ARF1) and secretion-associated RAS superfamily 1 (SAR1) GTP-binding proteins are involved in the formation and budding of vesicles throughout plant endomembrane systems. ARF1 has been shown to play a critical role in coat protein complex I (COPI)-mediated retrograde trafficking in eukaryotic systems, whereas SAR1 GTPases are involved in intracellular coat protein complex II (COPII)-mediated protein trafficking from the endoplasmic reticulum (ER) to the Golgi apparatus. The dysfunction of the endomembrane system can affect signal transduction, plant development, and defense. This chapter offers a summary of membrane trafficking system with an emphasis on the role of GTPases especially ARF1, SAR1, and RAB, their regulatory proteins, and interaction with endomembrane compartments. The vacuolar and endocytic trafficking are presented to enhance our understanding of plant development and immunity in plants.
Part of the book: Electrodialysis