| First Author | Fisher RP | Year | 1995 |
| Journal | Cell | Volume | 83 |
| Issue | 1 | Pages | 47-57 |
| PubMed ID | 7553872 | Mgi Jnum | J:29185 |
| Mgi Id | MGI:76716 | Doi | 10.1016/0092-8674(95)90233-3 |
| Citation | Fisher RP, et al. (1995) Alternative mechanisms of CAK assembly require an assembly factor or an activating kinase. Cell 83(1):47-57 |
| abstractText | We have cloned a mouse cDNA that encodes p36, a novel subunit of the CDK-activating kinase (CAK). p36 contains a C3HC4 zinc-binding domain or RING factor and is associated both with a TFIIH-bound form of CAK and with a free trimeric form. p36 promotes the assembly of CDK7 and cyclin H in vitro, stabilizing the transient CDK7-cyclin H complex. Stabilization and activation of CAK by p36 is independent of the phosphorylation state of T170, the conserved activating residue of CDK7. Assembly of active CDK7-cyclin H dimers can also occur through an alternative p36-independent pathway that requires phosphorylation of T170 by a CAK-activating kinase, or CAKAK. Thus, CDK7-cyclin H complex formation can be achieved by multiple mechanisms. |
