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

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.

Pubmed ID: 20702581


  • Davies BA
  • Azmi IF
  • Payne J
  • Shestakova A
  • Horazdovsky BF
  • Babst M
  • Katzmann DJ


Molecular biology of the cell

Publication Data

October 1, 2010

Associated Grants

  • Agency: NIGMS NIH HHS, Id: R01 GM073024
  • Agency: NIGMS NIH HHS, Id: R01 GM073024
  • Agency: NIGMS NIH HHS, Id: R01 GM074171

Mesh Terms

  • Adenosine Triphosphatases
  • Adenosine Triphosphate
  • Cell Membrane
  • Endosomal Sorting Complexes Required for Transport
  • Hydrolysis
  • Models, Biological
  • Mutant Proteins
  • Protein Stability
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Protein Subunits
  • Protein Transport
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Substrate Specificity