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Common mode of remodeling AAA ATPases p97/CDC48 by their disassembling cofactors ASPL/PUX1

Item Type:Article
Title:Common mode of remodeling AAA ATPases p97/CDC48 by their disassembling cofactors ASPL/PUX1
Creators Name:Banchenko, S. and Arumughan, A. and Petrović, S. and Schwefel, D. and Wanker, E.E. and Roske, Y. and Heinemann, U.
Abstract:The hexameric ring structure of the type II AAA+ ATPases is considered as stable and permanent. Recently, the UBX domain-containing cofactors Arabidopsis thaliana PUX1 and human alveolar soft part sarcoma locus (ASPL) were reported to bind and disassemble the cognate AAA+ ATPases AtCDC48 and human p97. Here, we present two crystal structures related to these complexes: a truncated AtCDC48 (AtCDC48-ND1) and a hybrid complex containing human p97-ND1 and the UBX domain of plant PUX1 (p97-ND1:PUX1-UBX). These structures reveal close similarity between the human and plant AAA+ ATPases, but also highlight differences between disassembling and non-disassembling AAA+ ATPase cofactors. Based on an AtCDC48 disassembly assay with PUX1 and known crystal structures of the p97-bound human cofactor ASPL, we propose a general ATPase disassembly model. Thus, our structural and biophysical investigations provide detailed insight into the mechanism of AAA+ ATPase disassembly by UBX domain cofactors and suggest a general mode of regulating the cellular activity of these molecular machines.
Keywords:p97 ATPase Regulation, CDC48, Ubiquitin Regulatory-X Domain, Pux1, Structural Remodeling
Source:Structure
ISSN:0969-2126
Publisher:Cell Press (U.S.A.)
Volume:27
Number:12
Page Range:1830-1841.e3
Date:3 December 2019
Official Publication:https://doi.org/10.1016/j.str.2019.10.001
PubMed:View item in PubMed

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