6hd3
Common mode of remodeling AAA ATPases p97/CDC48 by their disassembly cofactors ASPL/PUX1Common mode of remodeling AAA ATPases p97/CDC48 by their disassembly cofactors ASPL/PUX1
Structural highlights
Function[CD48A_ARATH] Probably functions in cell division and growth processes. Interacts with certain SNAREs as part of specialized membrane fusion events where vesicles from the same organelle fuse (homotypic fusion) (By similarity). Publication Abstract from PubMedThe 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. Common Mode of Remodeling AAA ATPases p97/CDC48 by Their Disassembling Cofactors ASPL/PUX1.,Banchenko S, Arumughan A, Petrovic S, Schwefel D, Wanker EE, Roske Y, Heinemann U Structure. 2019 Oct 21. pii: S0969-2126(19)30342-9. doi:, 10.1016/j.str.2019.10.001. PMID:31648844[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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