Yeast dynamin implicated in endocytic scission and the disassembly of endocytic components
The yeast dynamin-related GTPase Vps1 has been implicated in a range of cellular functions including vacuolar protein sorting, protein trafficking, organization of peroxisome, and endocytosis.1-2 Vps1 is present at endocytic sites and may be directly involved in endocytic vesicle invagination through its membrane-tubulating activity. Here, evidence supporting the functional link between Vps1 and the yeast amphiphysin Rvs167 in vesicle invagination is discussed. Though the disassembly of endocytic factors from pinched-off endocytic vesicles appears to be tightly regulated in a spatiotemporal manner, we are far from having complete understanding of the underlying mechanism. In this study, we provide evidence that Vps1 plays a role in the uncoating of endocytic proteins from post-internalized vesicles, based on the observation of a quick disassembly of two endocytic coat proteins Ent1 and Ent2 in cells lacking Vps1.
Copyright © 2011 Landes Bioscience.
Wang, Daobing, Jeff Sletto, Brandon Tenay, and Kyoungtae Kim. "Yeast dynamin implicated in endocytic scission and the disassembly of endocytic components." Communicative & integrative biology 4, no. 2 (2011): 178-181.
Communicative & Integrative Biology