Vps20p and Vta1p interact with Vps4p and function in multivesicular body sorting and endosomal transport in Saccharomyces cerevisiae

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Title Vps20p and Vta1p interact with Vps4p and function in multivesicular body sorting and endosomal transport in Saccharomyces cerevisiae
Author Yeo, Sebastian C. L.; Xu, Linghui; Ren, Jihui; Boulton, Victoria J.; Wagle, Mahendra D.; Liu, Cong; Ren, Gang; Wong, Peisze; Zahn, Regina; Sasajala, Piriya; Yang, Hongyuan; Piper, Robert C.; Munn, Alan L.
Journal Name Journal of Cell Science
Year Published 2003
Place of publication Cambridge, UK
Publisher The Company of Biologists
Abstract Vps4p (End13p) is an AAA-family ATPase that functions in membrane transport through endosomes, sorting of soluble vacuolar proteins to the vacuole, and multivesicular body (MVB) sorting of membrane proteins to the vacuole lumen. In a yeast two-hybrid screen with Vps4p as bait we isolated VPS20 (YMR077c) and the novel open reading frame YLR181c, for which the name VTA1 has recently been assigned (Saccharomyces Genome Database). Vps4p directly binds Vps20p and Vta1p in vitro and binding is not dependent on ATP - conversely, Vps4p binding to Vps20p is partially sensitive to ATP hydrolysis. Both ATP binding [Vps4p-(K179A)] and ATP hydrolysis [Vps4p-(E233Q)] mutant proteins exhibit enhanced binding to Vps20p and Vta1p in vitro. The Vps4p-Vps20p interaction involves the coiled-coil domain of each protein, whereas the Vps4p-Vta1p interaction involves the (non-coiled-coil) C-terminus of each protein. Deletion of either VPS20 (vps20) or VTA1 (vta1) leads to similar class E Vps- phenotypes resembling those of vps4, including carboxypeptidase Y (CPY) secretion, a block in ubiquitin-dependent MVB sorting, and a delay in both post-internalisation endocytic transport and biosynthetic transport to the vacuole. The vacuole resident membrane protein Sna3p (whose MVB sorting is ubiquitin-independent) does not appear to exit the class E compartment or reach the vacuole in cells lacking Vps20p, Vta1p or Vps4p, in contrast to other proteins whose delivery to the vacuole is only delayed. We propose that Vps20p and Vta1p regulate Vps4p function in vivo.
Peer Reviewed Yes
Published Yes
Alternative URI http://dx.doi.org/10.1242/jcs.00751
Volume 116
Page from 3957
Page to 3970
ISSN 0021-9533
Date Accessioned 2009-09-14
Language en_AU
Research Centre Griffith Health Institute; Molecular Basis of Disease
Faculty Griffith Health Faculty
Subject PRE2009-Biochemistry and Cell Biology
URI http://hdl.handle.net/10072/27162
Publication Type Journal Articles (Refereed Article)
Publication Type Code c1x

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