A switch point in the molecular chaperone Hsp90 responding to client interaction
نویسندگان
چکیده
منابع مشابه
The Interaction Network of the Hsp90 Molecular Chaperone
P. Wong · E. R. M. Tillier Department of Medical Biophysics , University of Toronto , Toronto , ON , Canada Abstract Heat shock protein 90 (Hsp 90) is a highly abundant and critical molecular chaperone that plays key roles in cellular quality control systems. The Hsp90 mechanism of function has been the subject of extensive investigation by many groups using traditional biochemical approaches a...
متن کاملClient-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex.
Hsp90 is an essential molecular chaperone required for the folding and activation of many hundreds of cellular "client" proteins. The ATP-dependent chaperone cycle involves significant conformational rearrangements of the Hsp90 dimer and interaction with a network of cochaperone proteins. Little is known about the mechanism of client protein binding or how cochaperone interactions modulate Hsp9...
متن کاملConformational dynamics of the molecular chaperone Hsp90.
The ubiquitous molecular chaperone Hsp90 makes up 1-2% of cytosolic proteins and is required for viability in eukaryotes. Hsp90 affects the folding and activation of a wide variety of substrate proteins including many involved in signaling and regulatory processes. Some of these substrates are implicated in cancer and other diseases, making Hsp90 an attractive drug target. Structural analyses h...
متن کاملThe Structure of the R2TP Complex Defines a Platform for Recruiting Diverse Client Proteins to the HSP90 Molecular Chaperone System
The R2TP complex, comprising the Rvb1p-Rvb2p AAA-ATPases, Tah1p, and Pih1p in yeast, is a specialized Hsp90 co-chaperone required for the assembly and maturation of multi-subunit complexes. These include the small nucleolar ribonucleoproteins, RNA polymerase II, and complexes containing phosphatidylinositol-3-kinase-like kinases. The structure and stoichiometry of yeast R2TP and how it couples ...
متن کاملA Primate Specific Extra Domain in the Molecular Chaperone Hsp90
Hsp90 (heat shock protein 90) is an essential molecular chaperone that mediates folding and quality control of client proteins. Many of them such as protein kinases, steroid receptors and transcription factors are involved in cellular signaling processes. Hsp90 undergoes an ATP hydrolysis dependent conformational cycle to assist folding of the client protein. The canonical Hsp90 shows a typical...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Nature Communications
سال: 2018
ISSN: 2041-1723
DOI: 10.1038/s41467-018-03946-x