Phosphorylation-driven epichaperome assembly is a regulator of cellular adaptability and proliferation.

ABSTRACT: The intricate network of protein-chaperone interactions is crucial for maintaining cellular function. Recent discoveries have unveiled the existence of specialized chaperone assemblies, known as epichaperomes, which serve as scaffolding platforms that orchestrate the reconfiguration of protein-protein interaction networks, thereby enhancing cellular adaptability and proliferation. This study explores the structural and regulatory aspects of epichaperomes, with a particular focus on the role of post-translational modifications (PTMs) in their formation and function. A key finding is the identification of specific PTMs on HSP90, particularly at residues Ser226 and Ser255 within an intrinsically disordered region, as critical determinants of epichaperome assembly. Our data demonstrate that ph

SUBMITTER: Roychowdhury T 

PROVIDER: S-EPMC11484706 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature