Common Mode of Remodeling AAA ATPases p97/CDC48 by Their Disassembling Cofactors ASPL/PUX1.
Structure
; 27(12): 1830-1841.e3, 2019 12 03.
Article
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| MEDLINE
| ID: mdl-31648844
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-ND1PUX1-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.
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MEDLINE
Asunto principal:
Proteínas Nucleares
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Proteínas Portadoras
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Arabidopsis
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Adenosina Trifosfatasas
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Coenzimas
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Proteínas de Ciclo Celular
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Proteínas de Arabidopsis
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Péptidos y Proteínas de Señalización Intracelular
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ATPasas Asociadas con Actividades Celulares Diversas
Idioma:
En
Año:
2019
Tipo del documento:
Article