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Asymmetric ring structure of Vps4 required for ESCRT-III disassembly.

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.
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Contributeur : Frank Thomas <>
Soumis le : jeudi 10 décembre 2015 - 09:06:54
Dernière modification le : mardi 8 décembre 2020 - 10:20:09

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Christophe Caillat, Pauline Macheboeuf, Yuanfei Wu, Andrew A Mccarthy, Elisabetta Boeri Erba, et al.. Asymmetric ring structure of Vps4 required for ESCRT-III disassembly.. Nature Communications, Nature Publishing Group, 2015, 6 (1), pp.8781. ⟨10.1038/ncomms9781⟩. ⟨hal-01241146⟩



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