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First published online September 2, 2003
doi: 10.1242/10.1242/jcs.00751

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Journal of Cell Science 116, 3957-3970 (2003)
doi: 10.1242/jcs.00751

Research Article

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

Sebastian C. L. Yeo1,{dagger}{dagger}, Linghui Xu1,{dagger}{dagger}, Jihui Ren2,*,{dagger}{dagger}, Victoria J. Boulton1, Mahendra D. Wagle1,{dagger}, Cong Liu1,{ddagger}, Gang Ren1,§, Peisze Wong1, Regina Zahn1,¶, Piriya Sasajala1,**, Hongyuan Yang2, Robert C. Piper3 and Alan L. Munn1,2,4,§,{ddagger}{ddagger}

1 Institute of Molecular and Cell Biology, The National University of Singapore, Singapore, 117609, Singapore
2 Department of Biochemistry, Faculty of Medicine, The National University of Singapore, Singapore, 119260, Singapore
3 Department of Physiology and Biophysics, University of Iowa, Iowa City, 52242, IA, USA
4 Institute for Molecular Bioscience, University of Queensland, Brisbane, QLD, 4072, Australia

{ddagger}{ddagger} Author for correspondence (e-mail: a.munn{at}imb.uq.edu.au)

Accepted 7 July 2003

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{Delta}) or VTA1 (vta1{Delta}) leads to similar class E Vps- phenotypes resembling those of vps4{Delta}, 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.

Key words: AAA-ATPase, Endocytosis, Endosome, Lysosome, LYST/beige, Chediak-Higashi syndrome




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