Asymmetric ring structure of Vps4 required for ESCRT-III disassembly

Christophe Caillat, Pauline Macheboeuf, Yuanfei Wu, Andrew A. McCarthy, Elisabetta Boeri-Erba, Gregory Effantin, Heinrich G. Göttlinger, Winfried Weissenhorn () and Patricia Renesto ()
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Christophe Caillat: Unit of Virus-Host Cell interactions (UVHCI), University of Grenoble Alpes
Pauline Macheboeuf: Unit of Virus-Host Cell interactions (UVHCI), University of Grenoble Alpes
Yuanfei Wu: Program in Gene Function and Expression, Program in Molecular Medicine, University of Massachusetts Medical School
Andrew A. McCarthy: Unit of Virus-Host Cell interactions (UVHCI), University of Grenoble Alpes
Elisabetta Boeri-Erba: Institut de Biologie Structurale (IBS), University of Grenoble Alpes
Gregory Effantin: Unit of Virus-Host Cell interactions (UVHCI), University of Grenoble Alpes
Heinrich G. Göttlinger: Program in Gene Function and Expression, Program in Molecular Medicine, University of Massachusetts Medical School
Winfried Weissenhorn: Unit of Virus-Host Cell interactions (UVHCI), University of Grenoble Alpes
Patricia Renesto: Unit of Virus-Host Cell interactions (UVHCI), University of Grenoble Alpes

Nature Communications, 2015, vol. 6, issue 1, 1-12

Abstract: Abstract The vacuolar protein sorting 4 AAA–ATPase (Vps4) recycles endosomal sorting complexes required for transport (ESCRT-III) polymers from cellular membranes. Here we present a 3.6-Å X-ray structure of ring-shaped Vps4 from Metallosphera sedula (MsVps4), seen as an asymmetric pseudohexamer. Conserved key interface residues are shown to be important for MsVps4 assembly, ATPase activity in vitro, ESCRT-III disassembly in vitro and HIV-1 budding. ADP binding leads to conformational changes within the protomer, which might propagate within the ring structure. All ATP-binding sites are accessible and the pseudohexamer binds six ATP with micromolar affinity in vitro. In contrast, ADP occupies one high-affinity and five low-affinity binding sites in vitro, consistent with conformational asymmetry induced on ATP hydrolysis. The structure represents a snapshot of an assembled Vps4 conformation and provides insight into the molecular motions the ring structure undergoes in a concerted action to couple ATP hydrolysis to ESCRT-III substrate disassembly.

Date: 2015
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DOI: 10.1038/ncomms9781

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