Scientific background: |
Hsp90 co-chaperone Cdc37, also called P50CDC37 is a protein that in humans is encoded by the CDC37 gene. The protein encoded by this gene is highly similar to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae. This gene is mapped to 19p13.2. This protein is a molecular chaperone with specific function in cell signal transduction. It has been shown to form complex with Hsp90 and a variety of protein kinases including CDK4, CDK6, SRC, RAF-1, MOK, as well as eIF2 alpha kinases. It is thought to play a critical role in directing Hsp90 to its target kinases. |
References: |
1. Chen, G., Cao, P., Goeddel, D. V. TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. Molec. Cell 9: 401-410, 2002.
2. Vaughan, C. K., Mollapour, M., Smith, J. R., Truman, A., Hu, B., Good, V. M., Panaretou, B., Neckers, L., Clarke, P. A., Workman, P., Piper, P. W., Prodromou, C., Pearl, L. H.Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37. Molec. Cell 31: 886-895, 2008.
|