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Yeast Dynamin Vps 1 and Amphiphysin Rvs 167 Function Together During Endocytosis
Author(s) -
Smaczynskade Rooij Iwona I.,
Allwood Ellen G.,
Mishra Ritu,
Booth Wesley I.,
Aghamohammadzadeh Soheil,
Goldberg Martin W.,
Ayscough Kathryn R.
Publication year - 2012
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/j.1600-0854.2011.01311.x
Subject(s) - endocytic cycle , dynamin , endocytosis , biology , microbiology and biotechnology , fusion protein , yeast , mutant , cytokinesis , biochemistry , receptor , gene , cell , recombinant dna , cell division
Dynamins are a conserved family of proteins involved in many membrane fusion and fission events. Previously, the dynamin‐related protein Vps 1 was shown to localize to endocytic sites, and yeast carrying deletions for genes encoding both the BAR domain protein Rvs 167 and Vps 1 had a more severe endocytic scission defect than either deletion alone. Vps 1 and Rvs 167 localize to endocytic sites at the onset of invagination and disassemble concomitant with inward vesicle movement. Rvs 167‐ GFP localization is reduced in cells lacking vps1 suggesting that Vps 1 influences Rvs 167 association with the endocytic complex. Unlike classical dynamins, Vps 1 does not have a proline–arginine domain that could interact with SH 3 domain‐containing proteins. Thus, while Rvs 167 has an SH 3 domain, it is not clear how an interaction would be mediated. Here, we demonstrate an interaction between Rvs 167 SH 3 domain and the single type I SH 3‐binding motif in Vps 1. Mutant Vps 1 that cannot bind Rvs 167 rescues all membrane fusion/fission functions associated with Vps 1 except for endocytic function, demonstrating the specificity and mechanistic importance of the interaction. In vitro , an Rvs 161/ Rvs 167 heterodimer can disassemble Vps 1 oligomers. Overall, the data support the idea that Vps 1 and the amphiphysins function together to mediate scission during endocytosis in yeast.