Disruption of Hsp90 leads to client protein degradation and often cell death. Heat shock protein 90 (Hsp90) is a molecular chaperone whose association is required for the stability and function of multiple mutated, chimeric and over-expressed signaling proteins that promote. Under stressful conditions, Hsp90 stabilizes its client proteins and provides protection to the cell against cellular stressors such as in cancer cells. Hsp90 fidelity of translation initiation intrinsically disordered regions molecular chaperone proteostasis. Heat shock protein 90 (Hsp90) is a molecular chaperone involved in the trafficking of proteins in the cell. Our study provides insights into how this abundant molecular chaperone supports a dynamic and healthy native protein landscape. We also discovered that Hsp90 controls the fidelity of ribosome initiation that triggers a heat shock response when disrupted. Hsp90 selectively utilized an IDR to regulate client activity as well as maintained IDR-protein health by preventing the transition to stress granules or P-bodies at physiological temperatures. Under normal growth conditions, Hsp90 plays a major role in various aspects of the secretory pathway and cellular transport during environmental stress, Hsp90. Activation of client protein kinases by the HSP90 molecular chaperone system is affected by phosphorylation at multiple sites on HSP90, the kinase-specific co-chaperone CDC37, and the. We found that Hsp90 associated with ∼20% of the yeast proteome using its three domains to preferentially target intrinsically disordered regions (IDRs) of client proteins. Using a chemical-biology approach, we characterized the features driving the Hsp90 physical interactome. An essential eukaryotic component of the chaperone system is Hsp90. Molecular chaperones govern proteome health to support cell homeostasis.

Hsp90 a molecular chaperone