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Activation of estrogen receptor alpha by S118 phosphorylation involves a ligand-dependent interaction with TFIIH and participation of CDK7.

Molecular cell | Jul 31, 2000

Phosphorylation of the estrogen receptor alpha (ERalpha) N-terminal transcription activation function AF1 at serine 118 (S118) modulates its activity. We show here that human ERalpha is phosphorylated by the TFIIH cyclin-dependent kinase in a ligand-dependent manner. Furthermore, the efficient phosphorylation of S118 requires a ligand-regulated interaction of TFIIH with AF2, the activation function located in the ligand binding domain (LBD) of ERalpha. This interaction involves (1) the integrity of helix 12 of the LBD/AF2 and (2) p62 and XPD, two subunits of the core TFIIH. These findings are suggestive of a novel mechanism by which nuclear receptor activity can be regulated by ligand-dependent recruitment of modifying activities, such as kinases.

Pubmed ID: 10949034 RIS Download

Mesh terms: Amino Acid Motifs | Amino Acid Sequence | Animals | Binding Sites | COS Cells | Cyclin-Dependent Kinases | Estrogen Receptor alpha | Humans | In Vitro Techniques | Ligands | Molecular Sequence Data | Phosphorylation | Protein Structure, Quaternary | Protein Structure, Tertiary | Protein-Serine-Threonine Kinases | Receptors, Estrogen | Recombinant Proteins | Serine | Transcription Factor TFIIH | Transcription Factors | Transcription Factors, TFII | Transcriptional Activation

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