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 o...

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Bibliographic Details
Published in:Molecular biology of the cell 2010-10, Vol.21 (19), p.3396-3408
Main Authors: Davies, Brian A, Azmi, Ishara F, Payne, Johanna, Shestakova, Anna, Horazdovsky, Bruce F, Babst, Markus, Katzmann, David J
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - chemistry
Adenosine Triphosphatases - metabolism
Adenosine Triphosphate - metabolism
Cell Membrane - metabolism
Endosomal Sorting Complexes Required for Transport - chemistry
Endosomal Sorting Complexes Required for Transport - metabolism
Hydrolysis
Models, Biological
Mutant Proteins - metabolism
Protein Stability
Protein Structure, Quaternary
Protein Structure, Tertiary
Protein Subunits - metabolism
Protein Transport
Saccharomyces cerevisiae - cytology
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - metabolism
Substrate Specificity
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Summary: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.
ISSN:1059-1524
1939-4586
DOI:10.1091/mbc.E10-06-0512