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TitleMultisystem Proteinopathy Mutations in VCP/p97 Increase NPLOC4·UFD1L Binding and Substrate Processing.
Journal, issue, pagesStructure, Vol. 27, Issue 12, Page 1820-11829.e4, Year 2019
Publish dateDec 3, 2019
AuthorsEmily E Blythe / Stephanie N Gates / Raymond J Deshaies / Andreas Martin /
PubMed AbstractValosin-containing protein (VCP)/p97 is an essential ATP-dependent protein unfoldase. Dominant mutations in p97 cause multisystem proteinopathy (MSP), a disease affecting the brain, muscle, and bone. ...Valosin-containing protein (VCP)/p97 is an essential ATP-dependent protein unfoldase. Dominant mutations in p97 cause multisystem proteinopathy (MSP), a disease affecting the brain, muscle, and bone. Despite the identification of numerous pathways that are perturbed in MSP, the molecular-level defects of these p97 mutants are not completely understood. Here, we use biochemistry and cryoelectron microscopy to explore the effects of MSP mutations on the unfoldase activity of p97 in complex with its substrate adaptor NPLOC4⋅UFD1L (UN). We show that all seven analyzed MSP mutants unfold substrates faster. Mutant homo- and heterohexamers exhibit tighter UN binding and faster substrate processing. Our structural studies suggest that the increased UN affinity originates from a decoupling of p97's nucleotide state and the positioning of its N-terminal domains. Together, our data support a gain-of-function model for p97-UN-dependent processes in MSP and underscore the importance of N-terminal domain movements for adaptor recruitment and substrate processing by p97.
External linksStructure / PubMed:31623962 / PubMed Central
MethodsEM (single particle)
Resolution4.26 Å
Structure data

EMDB-20730:
Cryo-EM structure of p97-A232E mutant bound to cofactors UFD1L and NPLOC4
Method: EM (single particle) / Resolution: 4.26 Å

Source
  • Homo sapiens (human)

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