Heat shock protein 82 (Hsp82)

Heat shock protein 82 (Hsp82) is a major molecular chaperone in the yeast *Saccharomyces cerevisiae*, essential for viability especially under heat or stress conditions[1][3][4][6]. It facilitates the correct folding, stability, and regulation of a wide range of client proteins involved in cell cycle control and signal transduction[4][5][6]. Hsp82, together with the highly similar Hsc82, forms an essential gene family whose proteins are structurally and functionally conserved across eukaryotes. Hsp82 is considered the yeast homolog of mammalian Hsp90, a critical target in cancer therapy research[1][5]. Hsp82 function is required at higher concentrations for cell growth at elevated temperatures; it binds a variety of cellular proteins, keeping them inactive until properly localized or activated[1][6]. Its chaperone activity is ATP-dependent and contributes to cytoprotection, protein quality control, and cell survival during physiological stress. Inhibitors of its human homolog are clinically significant in oncology, while the yeast Hsp82 is widely used as a model for understanding Hsp90 biology and drug action[2][5]. Caveats: - Hsp82 is *S. cerevisiae* (yeast) specific; in humans, the functionally analogous protein is heat shock protein 90 (Hsp90)[5]. - Drug and clinical relevance applies primarily to Hsp90, but yeast Hsp82 is a validated experimental surrogate in basic and translational research. If requesting information relevant to human targets, the canonical target would be "Heat shock protein 90 (Hsp90)" rather than Hsp82. Otherwise, this entry accurately characterizes the yeast Hsp82.

Other names

Hsp82Hsp90 (homologous human protein; see below for clarification)Heat shock protein HSP82Hsc82 (closely related yeast paralog)

Inhibition of chaperone activity (e.g., geldanamycin binds the ATPase domain, blocking proper folding and maturation of client proteins)