Asymmetric ring structure of Vps4 required for ESCRT-III disassembly. - Université Grenoble Alpes Accéder directement au contenu
Article Dans Une Revue Nature Communications Année : 2015

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

Résumé

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.

Dates et versions

hal-01241146 , version 1 (10-12-2015)

Identifiants

Citer

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, 2015, 6 (1), pp.8781. ⟨10.1038/ncomms9781⟩. ⟨hal-01241146⟩
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