Conformational changes in the AAA ATPase p97-p47 adaptor complex

Fabienne Beuron; Ingrid Dreveny; Xuemei Yuan; Valerie E. Pye; Ciaran Mckeown; Louise C. Briggs; Matthew J. Cliff; Yayoi Kaneko; Russell Wallis; Rivka L. Isaacson; John E. Ladbury; Steve J. Matthews; Hisao Kondo; Xiaodong Zhang; Paul S. Freemont

doi:10.1038/sj.emboj.7601055

Conformational changes in the AAA ATPase p97-p47 adaptor complex

Fabienne Beuron, Ingrid Dreveny, Xuemei Yuan, Valerie E. Pye, Ciaran Mckeown, Louise C. Briggs, Matthew J. Cliff, Yayoi Kaneko, Russell Wallis, Rivka L. Isaacson, John E. Ladbury, Steve J. Matthews, Hisao Kondo, Xiaodong Zhang, Paul S. Freemont

Research output: Contribution to journal › Article › peer-review

92 Citations (Scopus)

Abstract

The AAA + ATPase p97/VCP, helped by adaptor proteins, exerts its essential role in cellular events such as endoplasmic reticulum-associated protein degradation or the reassembly of Golgi, ER and the nuclear envelope after mitosis. Here, we report the three-dimensional cryo-electron microscopy structures at ∼20 Å resolution in two nucleotide states of the endogenous hexameric p97 in complex with a recombinant p47 trimer, one of the major p97 adaptor proteins involved in membrane fusion. Depending on the nucleotide state, we observe the p47 trimer to be in two distinct arrangements on top of the p97 hexamer. By combining the EM data with NMR and other biophysical measurements, we propose a model of ATP-dependent p97(N) domain motions that lead to a rearrangement of p47 domains, which could result in the disassembly of target protein complexes.

Original language	English
Pages (from-to)	1967-1976
Number of pages	10
Journal	EMBO Journal
Volume	25
Issue number	9
DOIs	https://doi.org/10.1038/sj.emboj.7601055
Publication status	Published - May 3 2006
Externally published	Yes

All Science Journal Classification (ASJC) codes

Neuroscience(all)
Molecular Biology
Biochemistry, Genetics and Molecular Biology(all)
Immunology and Microbiology(all)

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title = "Conformational changes in the AAA ATPase p97-p47 adaptor complex",

abstract = "The AAA + ATPase p97/VCP, helped by adaptor proteins, exerts its essential role in cellular events such as endoplasmic reticulum-associated protein degradation or the reassembly of Golgi, ER and the nuclear envelope after mitosis. Here, we report the three-dimensional cryo-electron microscopy structures at ∼20 {\AA} resolution in two nucleotide states of the endogenous hexameric p97 in complex with a recombinant p47 trimer, one of the major p97 adaptor proteins involved in membrane fusion. Depending on the nucleotide state, we observe the p47 trimer to be in two distinct arrangements on top of the p97 hexamer. By combining the EM data with NMR and other biophysical measurements, we propose a model of ATP-dependent p97(N) domain motions that lead to a rearrangement of p47 domains, which could result in the disassembly of target protein complexes.",

author = "Fabienne Beuron and Ingrid Dreveny and Xuemei Yuan and Pye, {Valerie E.} and Ciaran Mckeown and Briggs, {Louise C.} and Cliff, {Matthew J.} and Yayoi Kaneko and Russell Wallis and Isaacson, {Rivka L.} and Ladbury, {John E.} and Matthews, {Steve J.} and Hisao Kondo and Xiaodong Zhang and Freemont, {Paul S.}",

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AU - Beuron, Fabienne

AU - Dreveny, Ingrid

AU - Yuan, Xuemei

AU - Pye, Valerie E.

AU - Mckeown, Ciaran

AU - Briggs, Louise C.

AU - Cliff, Matthew J.

AU - Kaneko, Yayoi

AU - Wallis, Russell

AU - Isaacson, Rivka L.

AU - Ladbury, John E.

AU - Matthews, Steve J.

AU - Kondo, Hisao

AU - Zhang, Xiaodong

AU - Freemont, Paul S.

PY - 2006/5/3

Y1 - 2006/5/3

N2 - The AAA + ATPase p97/VCP, helped by adaptor proteins, exerts its essential role in cellular events such as endoplasmic reticulum-associated protein degradation or the reassembly of Golgi, ER and the nuclear envelope after mitosis. Here, we report the three-dimensional cryo-electron microscopy structures at ∼20 Å resolution in two nucleotide states of the endogenous hexameric p97 in complex with a recombinant p47 trimer, one of the major p97 adaptor proteins involved in membrane fusion. Depending on the nucleotide state, we observe the p47 trimer to be in two distinct arrangements on top of the p97 hexamer. By combining the EM data with NMR and other biophysical measurements, we propose a model of ATP-dependent p97(N) domain motions that lead to a rearrangement of p47 domains, which could result in the disassembly of target protein complexes.

AB - The AAA + ATPase p97/VCP, helped by adaptor proteins, exerts its essential role in cellular events such as endoplasmic reticulum-associated protein degradation or the reassembly of Golgi, ER and the nuclear envelope after mitosis. Here, we report the three-dimensional cryo-electron microscopy structures at ∼20 Å resolution in two nucleotide states of the endogenous hexameric p97 in complex with a recombinant p47 trimer, one of the major p97 adaptor proteins involved in membrane fusion. Depending on the nucleotide state, we observe the p47 trimer to be in two distinct arrangements on top of the p97 hexamer. By combining the EM data with NMR and other biophysical measurements, we propose a model of ATP-dependent p97(N) domain motions that lead to a rearrangement of p47 domains, which could result in the disassembly of target protein complexes.

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EP - 1976

JO - EMBO Journal

JF - EMBO Journal

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ER -

Conformational changes in the AAA ATPase p97-p47 adaptor complex

Abstract

All Science Journal Classification (ASJC) codes

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