P08238

HSP90 plays a crucial role as a molecular chaperone, assisting in proper folding and stabilization of numerous client proteins, including steroid hormone receptors and kinases, which are vital for cellular signaling and stress responses. This chaperoning function helps maintain cellular homeostasis and protects cells from stress-induced damage, thereby influencing processes such as cell growth, differentiation, and apoptosis. HSP90 forms complexes with various proteins, including glucocorticoid receptor, which is rendered transcriptionally inactive in the absence of ligand, highlighting HSP90′s role in regulating gene expression. HSP90′s ability to interact with a diverse array of proteins underscores HSP90′s significance in cellular function and potential as a therapeutic target in diseases characterized by protein misfolding and aggregation.