| First Author | Hunter T | Year | 1997 |
| Journal | Trends Cell Biol | Volume | 7 |
| Issue | 4 | Pages | 157-61 |
| PubMed ID | 17708934 | Mgi Jnum | J:39097 |
| Mgi Id | MGI:86478 | Doi | 10.1016/S0962-8924(97)01027-1 |
| Citation | Hunter T, et al. (1997) Cdc37: a protein kinase chaperone?. Trends Cell Biol 7(4):157-61 |
| abstractText | The activity of most protein kinases is highly regulated, typically via phosphorylation and/or subunit association. However, the folding of protein kinases into an active state or a form capable of activation is now emerging as another important step through which they can be regulated. The 50-kDa protein Cdc37 and the associated heat-shock protein Hsp90 have been found to bind to, and be required for the activity of, diverse protein kinases, including Cdk4, v-Src, Raf and SEVENLESS. Together, Cdc37 and Hsp90 may act as a general chaperone for protein kinases, in particular those involved in signal-transduction pathways and cell-cycle control. |
