Interaction between cyclin T1 and SCF(SKP2) targets CDK9 for ubiquitination and degradation by the proteasome.
Mol Cell Biol
; 21(23): 7956-70, 2001 Dec.
Article
en En
| MEDLINE
| ID: mdl-11689688
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Cisteína Endopeptidasas
/
Ubiquitinas
/
Ciclinas
/
Quinasas Ciclina-Dependientes
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Complejos de Ubiquitina-Proteína Ligasa
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Ligasas
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Complejos Multienzimáticos
Límite:
Animals
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Humans
Idioma:
En
Revista:
Mol Cell Biol
Año:
2001
Tipo del documento:
Article
País de afiliación:
Francia