Coordination of substrate binding and ATP hydrolysis in Vps4-mediated ESCRT-III disassembly

Brian A. Davies, Ishara F. Azmi, Johanna Payne, Anna Shestakova, Bruce F. Horazdovsky, Markus Babst, David J. Katzmann

Research output: Contribution to journalArticle

35 Scopus citations

Abstract

ESCRT-III undergoes dynamic assembly and disassembly to facilitate membrane exvagination processes including multivesicular body (MVB) formation, enveloped virus budding, and membrane abscission during cytokinesis. The AAA-ATPase Vps4 is required for ESCRT-III disassembly, however the coordination of Vps4 ATP hydrolysis with ESCRT-III binding and disassembly is not understood. Vps4 ATP hydrolysis has been proposed to execute ESCRT-III disassembly as either a stable oligomer or an unstable oligomer whose dissociation drives ESCRT-III disassembly. An in vitro ESCRT-III disassembly assay was developed to analyze Vps4 function during this process. The studies presented here support a model in which Vps4 acts as a stable oligomer during ATP hydrolysis and ESCRT-III disassembly. Moreover, Vps4 oligomer binding to ESCRT-III induces coordination of ATP hydrolysis at the level of individual Vps4 subunits. These results suggest that Vps4 functions as a stable oligomer that acts upon individual ESCRT-III subunits to facilitate ESCRT-III disassembly.

Original languageEnglish (US)
Pages (from-to)3396-3408
Number of pages13
JournalMolecular biology of the cell
Volume21
Issue number19
DOIs
StatePublished - Oct 1 2010

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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