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. 2012 Jul 25;5(8):779–801. doi: 10.3390/ph5080779

Table 1.

Co-chaperones of Hsp90.

Co-chaperone Function
Cdc37 Interacts with protein kinases
p23 Facilitates the maturation of client proteins
Aha1 Stimulates Hsp90 ATPase activity
SGT1 Binds to Hsp90 N-terminal domain, and inhibits Hsp90 ATPase activity
HOP Delivers steroid hormone receptor clients to Hsp90, and also mediates the binding of Hsp90 and Hsp70
TAH1 TPR containing protein, inhibits Hsp90 ATPase activity by forming cochaperone complex with PIH1
CHIP Is an E3 ubiquitin ligase, and regulates the balance of folding/degradation for Hsp90 clients
FKBP51/52 Mediates the interaction of steroid receptor with Hsp90

TAH1, TPR-containing protein associated with Hsp90; TPR, TetratricoPeptide Repeat; PIH1, protein interacting with Hsp90; CHIP, Carboxyl terminus of Hsc70-interacting protein; FKBP, FK506-binding protein.