In Vivo Conformational Dynamics of Hsp90 and Its Interactors.

ABSTRACT: Hsp90 belongs to a family of some of the most highly expressed heat shock proteins that function as molecular chaperones to protect the proteome not only from the heat shock but also from other misfolding events. As many client proteins of Hsp90 are involved in oncogenesis, this chaperone has been the focus of intense research efforts. Yet, we lack structural information for how Hsp90 interacts with co-chaperones and client proteins. Here, we developed a mass-spectrometry-based approach that allowed quantitative measurements of in vitro and in vivo effects of small-molecule inhibitors on Hsp90 conformation, and interaction with co-chaperones and client proteins. From this analysis, we were able to derive structural models for how Hsp90 engages its interaction partners in vivo, and how diff

SUBMITTER: Chavez JD 

PROVIDER: S-EPMC5012217 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature