• Register
X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

X

Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.

No
Yes

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

Authors

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

Journal

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