Abstract

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.

Department(s)

Biology

Document Type

Article

Additional Information

Addendum to: Nannapaneni S, Wang D, Jain S, Schroeder B, Highfill C, Reustle L, et al. The yeast dynamin-like protein Vps1:vps1 mutations perturb the internalization and the motility of endocytic vesicles and endosomes via disorganization of the actin cytoskeleton. European Journal of Cell Biology 2010; 89:499-508; PMID: 20189679; DOI:10.1016/j.ejcb.2010.02.002.

DOI

https://doi.org/10.4161/cib.4.2.14257

Rights Information

Copyright © 2011 Landes Bioscience.

Publication Date

2011

Journal Title

Communicative & Integrative Biology

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