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Mol Cell Biol. 2001 Dec;21(23):7956-70.

Interaction between cyclin T1 and SCF(SKP2) targets CDK9 for ubiquitination and degradation by the proteasome.

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1
Laboratoire de Virologie Moléculaire et Transfert de Gène, Institut de Génétique Humaine, UPR1142, Montpellier, France. rkiernan@igh.cnrs.fr

Abstract

CDK9 paired with cyclin T1 forms the human P-TEFb complex and stimulates productive transcription through phosphorylation of the RNA polymerase II C-terminal domain. Here we report that CDK9 is ubiquitinated and degraded by the proteasome whereas cyclin T1 is stable. SCF(SKP2) was recruited to CDK9/cyclin T1 via cyclin T1 in an interaction requiring its PEST domain. CDK9 ubiquitination was modulated by cyclin T1 and p45(SKP2). CDK9 accumulated in p45(SKP2-/-) cells, and its expression during the cell cycle was periodic. The transcriptional activity of CDK9/cyclin T1 on the class II major histocompatibility complex promoter could be regulated by CDK9 degradation in vivo. We propose a novel mechanism whereby recruitment of SCF(SKP2) is mediated by cyclin T1 while ubiquitination occurs exclusively on CDK9.

PMID:
11689688
PMCID:
PMC99964
DOI:
10.1128/MCB.21.23.7956-7970.2001
[Indexed for MEDLINE]
Free PMC Article
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