Ontology highlight
ABSTRACT:
SUBMITTER: Keramisanou D
PROVIDER: S-EPMC8926337 | biostudies-literature | 2022 Mar
REPOSITORIES: biostudies-literature
Keramisanou Dimitra D Vasantha Kumar M V MV Boose Nicole N Abzalimov Rinat R RR Gelis Ioannis I
Science advances 20220316 11
Molecular chaperones have an essential role for the maintenance of a balanced protein homeostasis. Here, we investigate how protein kinases are recruited and loaded to the Hsp90-Cdc37 complex, the first step during Hsp90-mediated chaperoning that leads to enhanced client kinase stability and activation. We show that conformational dynamics of all partners is a critical feature of the underlying loading mechanism. The kinome co-chaperone Cdc37 exists primarily in a dynamic extended conformation b ...[more]