TFIIH interacts with the retinoic acid receptor γ and phosphorylates its AF-1-activating domain through cdk7

被引：88

作者：

Bastien, J ^{[1
]}

Adam-Stitah, S ^{[1
]}

Riedl, T ^{[1
]}

Egly, JM ^{[1
]}

Chambon, P ^{[1
]}

Rochette-Egly, C ^{[1
]}

机构：

[1] Univ Strasbourg 1, Coll France, INSERM, CNRS,Inst Genet & Biol Mol & Cellulaire, F-67404 Illkirch Graffenstaden, France

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2000年 / 275卷 / 29期

关键词：

D O I：

10.1074/jbc.M001985200

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Retinoic acid receptor gamma (RAR gamma) is phosphorylated in COS-1 cells at two conserved serine residues located in the N-terminal region (serines 77 and 79 in RAR gamma 1 and serines 66 and 68 in RAR gamma 2) that contains the activation function AF-1. These serines are phosphorylated in vitro by cdk7, a cyclin-dependent kinase associated to cyclin H and MAT1 in the CAK complex (cdk7 cyclin H MAT1), that is found either free or as a component of the transcription/DNA repair factor TFIIH, RAR gamma is more efficiently phosphorylated by TFIIH than by CAK. and interacts not only with cdk7 but also with several additional subunits of TFIIH. RAR gamma phosphorylation and interaction with TFIIH occur in a ligand-independent manner. Our data demonstrate also that phosphorylation of the AF-1 function modulates RAR gamma transcriptional activity in a response gene-dependent manner.

引用

页码：21896 / 21904

页数：9

共 56 条

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