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Published 27 February 2006. doi:10.1083/jcb.200508166
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 172, Number 5, 705-717
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Article

Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1



Ishara Azmi1, Brian Davies1, Christian Dimaano2, Johanna Payne1, Debra Eckert3, Markus Babst2, and David J. Katzmann1

1 Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Rochester, MN 55905
2 Department of Biology and 3 Department of Biochemistry, University of Utah, Salt Lake City, UT 84112

Correspondence to Markus Babst: babst{at}biology.utah.edu; or David J. Katzmann:katzmann.david{at}mayo.edu

In eukaryotes, the multivesicular body (MVB) sorting pathway plays an essential role in regulating cell surface protein composition, thereby impacting numerous cellular functions. Vps4, an ATPase associated with a variety of cellular activities, is required late in the MVB sorting reaction to dissociate the endosomal sorting complex required for transport (ESCRT), a requisite for proper function of this pathway. However, regulation of Vps4 function is not understood. We characterize Vta1 as a positive regulator of Vps4 both in vivo and in vitro. Vta1 promotes proper assembly of Vps4 and stimulates its ATPase activity through the conserved Vta1/SBP1/LIP5 region present in Vta1 homologues across evolution, including human SBP1 and Arabidopsis thaliana LIP5. These results suggest an evolutionarily conserved mechanism through which the disassembly of the ESCRT proteins, and thereby MVB sorting, is regulated by the Vta1/SBP1/LIP5 proteins.

Abbreviations used in this paper: CPS, carboxypeptidase S; ESCRT, endosomal sorting complex required for transport; hSPB1, human SPB1; MVB, multivesicular body; PtdIns(3)P, phosphatidylinositol-3-phosphate; Vps, vacuolar protein sorting; VSL, Vta1/SBP1/LIP5.


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