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.
Main Authors: | 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 |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2018-04-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-018-03942-1 |
Similar Items
-
Author Correction: RPAP3 provides a flexible scaffold for coupling HSP90 to the human R2TP co-chaperone complex
by: Fabrizio Martino, et al.
Published: (2018-07-01) -
The structure of FKBP38 in complex with the MEEVD tetratricopeptide binding-motif of Hsp90.
by: Katie L I M Blundell, et al.
Published: (2017-01-01) -
RPAP3 C-Terminal Domain: A Conserved Domain for the Assembly of R2TP Co-Chaperone Complexes
by: Carlos F. Rodríguez, et al.
Published: (2020-05-01) -
The RPAP3-Cterminal domain identifies R2TP-like quaternary chaperones
by: Chloé Maurizy, et al.
Published: (2018-05-01) -
HECTD3 Mediates an HSP90-Dependent Degradation Pathway for Protein Kinase Clients
by: Zhaobo Li, et al.
Published: (2017-06-01)