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

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.

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Autores principales:	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
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/817fe8022b364f6ab87e9c148af5e6d8
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spelling	oai:doaj.org-article:817fe8022b364f6ab87e9c148af5e6d82021-12-02T14:39:08ZRPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex10.1038/s41467-018-03942-12041-1723https://doaj.org/article/817fe8022b364f6ab87e9c148af5e6d82018-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-03942-1https://doaj.org/toc/2041-1723The 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.Fabrizio MartinoMohinder PalHugo Muñoz-HernándezCarlos F. RodríguezRafael Núñez-RamírezDavid Gil-CartonGianluca DegliespostiJ. Mark SkehelS. Mark RoeChrisostomos ProdromouLaurence H. PearlOscar LlorcaNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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 RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex
description	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.
format	article
author	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
author_facet	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
author_sort	Fabrizio Martino
title	RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex
title_short	RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex
title_full	RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex
title_fullStr	RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex
title_full_unstemmed	RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex
title_sort	rpap3 provides a flexible scaffold for coupling hsp90 to the human r2tp co-chaperone complex
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/817fe8022b364f6ab87e9c148af5e6d8
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RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex

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