RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex

Fabrizio Martino; Mohinder Pal; Hugo Muñoz-Hernández; Carlos F. Rodríguez; Rafael Núñez-Ramírez; David Gil-Carton; Gianluca Degliesposti; J. Mark Skehel; S. Mark Roe; Chrisostomos Prodromou; Laurence H. Pearl; Oscar Llorca

doi:10.1038/s41467-018-03942-1

Nature Communications (Apr 2018)

RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex

Fabrizio Martino,
Mohinder Pal,
Hugo Muñoz-Hernández,
Carlos F. Rodríguez,
Rafael Núñez-Ramírez,
David Gil-Carton,
Gianluca Degliesposti,
J. Mark Skehel,
S. Mark Roe,
Chrisostomos Prodromou,
Laurence H. Pearl,
Oscar Llorca

Affiliations

Fabrizio Martino: Centro de Investigaciones Biológicas (CIB), Spanish National Research Council (CSIC)
Mohinder Pal: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer
Hugo Muñoz-Hernández: Centro de Investigaciones Biológicas (CIB), Spanish National Research Council (CSIC)
Carlos F. Rodríguez: Centro de Investigaciones Biológicas (CIB), Spanish National Research Council (CSIC)
Rafael Núñez-Ramírez: Centro de Investigaciones Biológicas (CIB), Spanish National Research Council (CSIC)
David Gil-Carton: Structural Biology Unit, CIC bioGUNE, Bizkaia Technology Park
Gianluca Degliesposti: MRC Laboratory of Molecular Biology, Cambridge Biomedical Campus
J. Mark Skehel: MRC Laboratory of Molecular Biology, Cambridge Biomedical Campus
S. Mark Roe: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer
Chrisostomos Prodromou: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer
Laurence H. Pearl: Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer
Oscar Llorca: Centro de Investigaciones Biológicas (CIB), Spanish National Research Council (CSIC)

DOI: https://doi.org/10.1038/s41467-018-03942-1
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 13

Abstract

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The R2TP/PFDL co-chaperone facilitates assembly of RNA polymerase II and PI3-kinase-like kinases such as mTOR by a so far unknown mechanism. Here authors provide the cryo-EM structure of human R2TP, which shows how RPAP3 serves as a flexible platform to recruit HSP90 to diverse client proteins.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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