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dc.contributor.authorC. L. Yeo, Sebastianen_US
dc.contributor.authorXu, Linghuien_US
dc.contributor.authorRen, Jihuien_US
dc.contributor.authorBoulton, Victoria J.en_US
dc.contributor.authorD. Wagle, Mahendraen_US
dc.contributor.authorLiu, Congen_US
dc.contributor.authorRen, Gangen_US
dc.contributor.authorWong, Peiszeen_US
dc.contributor.authorZahn, Reginaen_US
dc.contributor.authorSasajala, Piriyaen_US
dc.contributor.authorYang, Hongyuanen_US
dc.contributor.authorC. Piper, Roberten_US
dc.contributor.authorL. Munn, Alanen_US
dc.date.accessioned2017-04-24T14:55:57Z
dc.date.available2017-04-24T14:55:57Z
dc.date.issued2003en_US
dc.date.modified2009-12-07T03:39:56Z
dc.identifier.issn0021-9533en_US
dc.identifier.doi10.1242/jcs.00751en_AU
dc.identifier.urihttp://hdl.handle.net/10072/27162
dc.description.abstractVps4p (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.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_AU
dc.languageEnglishen_US
dc.language.isoen_AU
dc.publisherThe Company of Biologistsen_US
dc.publisher.placeCambridge, UKen_US
dc.relation.ispartofpagefrom3957en_US
dc.relation.ispartofpageto3970en_US
dc.relation.ispartofjournalJournal of Cell Scienceen_US
dc.relation.ispartofvolume116en_US
dc.subject.fieldofresearchcode270199en_US
dc.titleVps20p and Vta1p interact with Vps4p and function in multivesicular body sorting and endosomal transport in Saccharomyces cerevisiaeen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.date.issued2003
gro.hasfulltextNo Full Text


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