Heat shock protein 90 kDa alpha, class B, member 1 (HSP90AB1)

Heat shock protein 90 kDa alpha, class B, member 1 (HSP90AB1) is a constitutively expressed molecular chaperone of the HSP90 family in the cytoplasm, responsible for ensuring proper folding, stabilization, degradation, and functional regulation of a large array of client proteins, especially those involved in cell cycle, signal transduction, and stress response. It operates as a homodimer with ATPase activity and interacts with a vast network of co-chaperones to maintain protein homeostasis. HSP90AB1 plays an essential role in enabling cells to survive stress and is heavily implicated in the maintenance and progression of various cancers due to its critical support of oncogenic partner proteins. This has made it a validated therapeutic target, with several drugs developed to inhibit its chaperone function, primarily through blocking its ATP-binding site, thereby destabilizing its client proteins and inducing apoptosis especially in cancer cells[1][2][3][4].

Other names

Heat shock protein HSP 90-betaHSP90-betaHSP90BHSPC2HSPCBHSP 90HSP 84HSP84Heat shock 84 kDaHeat shock protein family C member 3D6S182

Inhibition of HSP90 ATPase activity disrupts client protein folding; Induces degradation of oncogenic client proteins; Alters cell signaling pathways, especially those linked to cancer cell survival