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Heat shock protein 90 chaperone complex

Molecular classification
Molecular chaperone complex
01

Overview

Heat shock protein 90 (Hsp90) is a highly conserved and essential molecular chaperone complex. It plays a central role in maintaining cellular proteostasis by assisting the folding, maturation, stabilization, activation, and degradation of a wide array of client proteins. Hsp90 is especially important under stress conditions but also has critical functions in unstressed cells. Its clients include many signaling molecules that regulate cell growth and survival, making it an attractive target for anti-cancer drug development.

Other names
HSP90 complexHeat shock protein 86 kDaRenal carcinoma antigen NY‑REN‑38
02

Mechanism of action

Inhibition of Hsp90 leads to degradation of oncogenic clients.

03

Biological functions

Protein foldingProtein maturationProtein stabilizationProtein degradationStress response
04

Disease associations

CancerNeurodegenerative disease

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