Mechanisms of vesicle formation: Insights from the COP system
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Cited by (91)
Molecular Simulation of Mechanical Properties and Membrane Activities of the ESCRT-III Complexes
2020, Biophysical JournalCitation Excerpt :The endosomal sorting complex required for transport (ESCRTs) proteins are cytosolic factors that are involved in fundamental cellular processes including organelle biogenesis (9,10), sorting cargo into intraluminal vesicles of multivesicular endosomes (11–13), cytokinesis (14–16), plasma membrane and lysosome repair (17–19), and the formation and scission of intraluminal vesicles (20–23), among many others (24–32). ESCRTs are of particular interest because the membrane curvature they induce results in budding away from the cytoplasm (Fig. 1 a), which is topologically opposite as compared to the vesicles formed by other proteins such as clathrin, COP-I, and COP-II (24,33–37). The core ESCRT machinery is composed of five complexes: ESCRT-0, -I, -II, and -III and the Vps4 AAA ATPase.
Activation machinery of the small GTPase Arf6
2014, Advances in Biological RegulationLipid-dependent protein sorting at the trans-Golgi network
2012, Biochimica et Biophysica Acta - Molecular and Cell Biology of LipidsThe transmembrane domain of the molecular chaperone cosmc directs its localization to the endoplasmic reticulum
2011, Journal of Biological ChemistryCitation Excerpt :The two major pathways of localizing proteins to the ER are retrieval from distal compartments back to ER by retrograde transport or retention through active exclusion from vesicles that exit the ER (6), and some proteins, such as the ER chaperone calreticulin (44), may utilize both retention and retrieval. ER retrieval systems include the C-terminal H/KDEL lumenal sequence (2, 3), which is recognized by the ERD2-like receptor in post-ER compartments, leading to formation of COPI-coated vesicles and eventual retrotranslocation to the ER (4, 5). Some ER-resident proteins carry other specific sequence motifs that interact with COPI complexes, such as di-lysine (K(X)KXX) (45, 46), di-arginine (RR or RXR) (10, 11), and di-phenylalanine (FF) (13, 14) that promote recruitment into COPI vesicle machinery for retrieval to the ER.
The TOR complex 1 is distributed in endosomes and in retrograde vesicles that form from the vacuole membrane and plays an important role in the vacuole import and degradation pathway
2010, Journal of Biological ChemistryCitation Excerpt :Purified Vid vesicles also contain COPI coatomer proteins (25). COPI vesicles are involved in multiple protein trafficking pathways including the retrograde trafficking from the Golgi to the endoplasmic reticulum, intra-Golgi trafficking, and endosomal trafficking (30–33). In mammalian cells and in yeast coatomer components are found on endosomes and play critical roles in endocytic trafficking and in multivesicular body sorting (34–39).