The Complex Phosphorylation Patterns that Regulate the Activity of Hsp70 and Its Cochaperones.

ABSTRACT: Proteins must fold into their native structure and maintain it during their lifespan to display the desired activity. To ensure proper folding and stability, and avoid generation of misfolded conformations that can be potentially cytotoxic, cells synthesize a wide variety of molecular chaperones that assist folding of other proteins and avoid their aggregation, which unfortunately is unavoidable under acute stress conditions. A protein machinery in metazoa, composed of representatives of the Hsp70, Hsp40, and Hsp110 chaperone families, can reactivate protein aggregates. We revised herein the phosphorylation sites found so far in members of these chaperone families and the functional consequences associated with some of them. We also discuss how phosphorylation might regulate the chaperone

SUBMITTER: Velasco L 

PROVIDER: S-EPMC6747476 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature