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| Item Type: | Article |
|---|---|
| Title: | Common mode of remodeling AAA ATPases p97/CDC48 by their disassembling cofactors ASPL/PUX1 |
| Creators Name: | Banchenko, S., Arumughan, A., Petrović, S., Schwefel, D., Wanker, E.E., 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 |
| Volume: | 27 |
| Number: | 12 |
| Page Range: | 1830-1841 |
| 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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