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dc.contributor.authorC. L. Yeo, Sebastian
dc.contributor.authorXu, Linghui
dc.contributor.authorRen, Jihui
dc.contributor.authorBoulton, Victoria J.
dc.contributor.authorD. Wagle, Mahendra
dc.contributor.authorLiu, Cong
dc.contributor.authorRen, Gang
dc.contributor.authorWong, Peisze
dc.contributor.authorZahn, Regina
dc.contributor.authorSasajala, Piriya
dc.contributor.authorYang, Hongyuan
dc.contributor.authorC. Piper, Robert
dc.contributor.authorL. Munn, Alan
dc.date.accessioned2017-05-03T16:59:01Z
dc.date.available2017-05-03T16:59:01Z
dc.date.issued2003
dc.date.modified2009-12-07T03:39:56Z
dc.identifier.issn0021-9533
dc.identifier.doi10.1242/jcs.00751
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.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherThe Company of Biologists
dc.publisher.placeCambridge, UK
dc.relation.ispartofpagefrom3957
dc.relation.ispartofpageto3970
dc.relation.ispartofjournalJournal of Cell Science
dc.relation.ispartofvolume116
dc.subject.fieldofresearchBiological Sciences
dc.subject.fieldofresearchMedical and Health Sciences
dc.subject.fieldofresearchcode06
dc.subject.fieldofresearchcode11
dc.titleVps20p and Vta1p interact with Vps4p and function in multivesicular body sorting and endosomal transport in Saccharomyces cerevisiae
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.date.issued2003
gro.hasfulltextNo Full Text
gro.griffith.authorMunn, Alan L.


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