CDC37
Description
The CDC37 (cell division cycle 37, HSP90 cochaperone) is a protein-coding gene located on chromosome 19.
CDC37 is a human protein encoded by the CDC37 gene. It shares high similarity to Cdc37, a cell division cycle control protein in Saccharomyces cerevisiae. As an HSP90 co-chaperone, CDC37 plays a key role in cell signal transduction. It forms complexes with Hsp90 and a variety of protein kinases including CDK4, CDK6, SRC, RAF1, MOK, and eIF-2 alpha kinases. CDC37 is thought to direct Hsp90 to these target kinases. CDC37 consists of three structural domains: the N-terminal domain, which binds to protein kinases; the central domain, which is the Hsp90 chaperone binding domain; and the C-terminal domain, whose function is unclear.
CDC37 acts as a co-chaperone, binding to various kinases and facilitating their interaction with the Hsp90 complex. This interaction results in the stabilization and enhanced activity of these kinases. Additionally, CDC37 inhibits the ATPase activity of HSP90AA1.
CDC37 is also known as P50CDC37.
