An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans.

ABSTRACT: Heat shock protein 90 (Hsp90) is an essential eukaryotic molecular chaperone. To properly chaperone its clientele, Hsp90 proceeds through an ATP-dependent conformational cycle influenced by posttranslational modifications (PTMs) and assisted by a number of co-chaperone proteins. Although Hsp90 conformational changes in solution have been well-studied, regulation of these complex dynamics in cells remains unclear. Phosphorylation of human Hsp90α at the highly conserved tyrosine 627 has previously been reported to reduce client interaction and Aha1 binding. Here we report that these effects are due to a long-range conformational impact inhibiting Hsp90α N-domain dimerization and involving a region of the middle domain/carboxy-terminal domain interface previously suggested to be a substrate b

SUBMITTER: Zuehlke AD 

PROVIDER: S-EPMC5458067 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature