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Heat shock protein 90 alpha (HSP90α) is a highly conserved, stress-inducible molecular chaperone that plays a central role in maintaining protein homeostasis, especially under conditions of proteotoxic stress. It supports cell survival by regulating key processes such as cell cycle control, hormone signaling pathways, apoptosis regulation, DNA repair, and signal transduction cascades. HSP90α stabilizes many oncogenic proteins and is overexpressed in various cancers, supporting tumor growth and progression. It is a therapeutic target for cancer, with inhibitors and antibodies being developed to disrupt its function.
Inhibition of ATP binding to HSP90, disruption of HSP90 chaperone function, inhibition of client protein stabilization
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