Journal article
Vps20p and Vta1p interact with Vps4p and function in multivesicular body sorting and endosomal transport in Saccharomyces cerevisiae
Journal of cell science, Vol.116(19), pp.3957-3970
10/01/2003
DOI: 10.1242/jcs.00751
PMID: 12953057
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 (vps20Δ) or VTA1 (vta1Δ) leads to similar class E Vps- phenotypes resembling those of vps4Δ, 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.
Details
- Title: Subtitle
- Vps20p and Vta1p interact with Vps4p and function in multivesicular body sorting and endosomal transport in Saccharomyces cerevisiae
- Creators
- Sebastian C. L. Yeo - National University of SingaporeLinghui Xu - National University of SingaporeJihui Ren - National University of SingaporeVictoria J. Boulton - National University of SingaporeMahendra D. Wagle - National University of SingaporeCong Liu - National University of SingaporeGang Ren - National University of SingaporePeisze Wong - National University of SingaporeRegina Zahn - National University of SingaporePiriya Sasajala - National University of SingaporeHongyuan Yang - National University of SingaporeRobert C. Piper - University of IowaAlan L. Munn - University of Queensland
- Resource Type
- Journal article
- Publication Details
- Journal of cell science, Vol.116(19), pp.3957-3970
- DOI
- 10.1242/jcs.00751
- PMID
- 12953057
- ISSN
- 0021-9533
- eISSN
- 1477-9137
- Language
- English
- Date published
- 10/01/2003
- Academic Unit
- Molecular Physiology and Biophysics; Medicine Administration; Internal Medicine
- Record Identifier
- 9984297607702771
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