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

http://www.ncbi.nlm.nih.gov/pubmed/20702581

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 RIS Download

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

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