Hsp90 co-chaperone Cdc37 (CDC37)

Hsp90 co-chaperone Cdc37 (CDC37) is a co-chaperone molecule that specifically mediates the interactions between Hsp90 and a wide range of protein kinases essential for cell signal transduction, cell cycle progression, and other regulated processes[2][3][5][6]. Its N-terminal domain binds to kinase clients, while its middle and C-terminal domains mediate interactions with Hsp90[3][5][6]. CDC37 stabilizes client kinases, assists in their folding and activation, and is implicated in the regulation of numerous oncogenic signaling pathways, including those involving CDK4, CDK6, SRC, and RAF1 kinases[3][5][6]. Overexpression or dysregulation can contribute to oncogenesis, making it a potential target for anticancer therapies, particularly in contexts where kinase signaling drives malignancy, although no clinically approved drugs target CDC37 directly at present[2][6].

Other names

Cdc37P50CDC37p50Cdc37CDC37Acell division cycle 37 homologHsp90 chaperone protein kinase-targeting subunit

Inhibition of Hsp90-CDC37 interaction (potential strategy under investigation); Disruption of client protein kinase maturation and stabilization