author_facet Davies, Brian A.
Azmi, Ishara F.
Payne, Johanna
Shestakova, Anna
Horazdovsky, Bruce F.
Babst, Markus
Katzmann, David J.
Davies, Brian A.
Azmi, Ishara F.
Payne, Johanna
Shestakova, Anna
Horazdovsky, Bruce F.
Babst, Markus
Katzmann, David J.
author Davies, Brian A.
Azmi, Ishara F.
Payne, Johanna
Shestakova, Anna
Horazdovsky, Bruce F.
Babst, Markus
Katzmann, David J.
spellingShingle Davies, Brian A.
Azmi, Ishara F.
Payne, Johanna
Shestakova, Anna
Horazdovsky, Bruce F.
Babst, Markus
Katzmann, David J.
Molecular Biology of the Cell
Coordination of Substrate Binding and ATP Hydrolysis in Vps4-Mediated ESCRT-III Disassembly
Cell Biology
Molecular Biology
author_sort davies, brian a.
spelling Davies, Brian A. Azmi, Ishara F. Payne, Johanna Shestakova, Anna Horazdovsky, Bruce F. Babst, Markus Katzmann, David J. 1059-1524 1939-4586 American Society for Cell Biology (ASCB) Cell Biology Molecular Biology http://dx.doi.org/10.1091/mbc.e10-06-0512 <jats:p> 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. </jats:p> Coordination of Substrate Binding and ATP Hydrolysis in Vps4-Mediated ESCRT-III Disassembly Molecular Biology of the Cell
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title Coordination of Substrate Binding and ATP Hydrolysis in Vps4-Mediated ESCRT-III Disassembly
title_unstemmed Coordination of Substrate Binding and ATP Hydrolysis in Vps4-Mediated ESCRT-III Disassembly
title_full Coordination of Substrate Binding and ATP Hydrolysis in Vps4-Mediated ESCRT-III Disassembly
title_fullStr Coordination of Substrate Binding and ATP Hydrolysis in Vps4-Mediated ESCRT-III Disassembly
title_full_unstemmed Coordination of Substrate Binding and ATP Hydrolysis in Vps4-Mediated ESCRT-III Disassembly
title_short Coordination of Substrate Binding and ATP Hydrolysis in Vps4-Mediated ESCRT-III Disassembly
title_sort coordination of substrate binding and atp hydrolysis in vps4-mediated escrt-iii disassembly
topic Cell Biology
Molecular Biology
url http://dx.doi.org/10.1091/mbc.e10-06-0512
publishDate 2010
physical 3396-3408
description <jats:p> 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. </jats:p>
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author Davies, Brian A., Azmi, Ishara F., Payne, Johanna, Shestakova, Anna, Horazdovsky, Bruce F., Babst, Markus, Katzmann, David J.
author_facet Davies, Brian A., Azmi, Ishara F., Payne, Johanna, Shestakova, Anna, Horazdovsky, Bruce F., Babst, Markus, Katzmann, David J., Davies, Brian A., Azmi, Ishara F., Payne, Johanna, Shestakova, Anna, Horazdovsky, Bruce F., Babst, Markus, Katzmann, David J.
author_sort davies, brian a.
container_issue 19
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container_title Molecular Biology of the Cell
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description <jats:p> 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. </jats:p>
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spelling Davies, Brian A. Azmi, Ishara F. Payne, Johanna Shestakova, Anna Horazdovsky, Bruce F. Babst, Markus Katzmann, David J. 1059-1524 1939-4586 American Society for Cell Biology (ASCB) Cell Biology Molecular Biology http://dx.doi.org/10.1091/mbc.e10-06-0512 <jats:p> 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. </jats:p> Coordination of Substrate Binding and ATP Hydrolysis in Vps4-Mediated ESCRT-III Disassembly Molecular Biology of the Cell
spellingShingle Davies, Brian A., Azmi, Ishara F., Payne, Johanna, Shestakova, Anna, Horazdovsky, Bruce F., Babst, Markus, Katzmann, David J., Molecular Biology of the Cell, Coordination of Substrate Binding and ATP Hydrolysis in Vps4-Mediated ESCRT-III Disassembly, Cell Biology, Molecular Biology
title Coordination of Substrate Binding and ATP Hydrolysis in Vps4-Mediated ESCRT-III Disassembly
title_full Coordination of Substrate Binding and ATP Hydrolysis in Vps4-Mediated ESCRT-III Disassembly
title_fullStr Coordination of Substrate Binding and ATP Hydrolysis in Vps4-Mediated ESCRT-III Disassembly
title_full_unstemmed Coordination of Substrate Binding and ATP Hydrolysis in Vps4-Mediated ESCRT-III Disassembly
title_short Coordination of Substrate Binding and ATP Hydrolysis in Vps4-Mediated ESCRT-III Disassembly
title_sort coordination of substrate binding and atp hydrolysis in vps4-mediated escrt-iii disassembly
title_unstemmed Coordination of Substrate Binding and ATP Hydrolysis in Vps4-Mediated ESCRT-III Disassembly
topic Cell Biology, Molecular Biology
url http://dx.doi.org/10.1091/mbc.e10-06-0512