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Bujnicki Lab Homepage

"Alternative mechanisms of CAK assembly require an assembly factor or an activating kinase."

Fisher RP, Jin P, Chamberlin HM, Morgan DO



Published Oct. 6, 1995 in Cell volume 83 .

Pubmed ID: 7553872

Abstract:
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.


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Last modification of this entry: Oct. 6, 2010

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