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Activation of estrogen receptor alpha by S118 phosphorylation involves a ligand-dependent interaction with TFIIH and participation of CDK7.
- Source :
-
Molecular cell [Mol Cell] 2000 Jul; Vol. 6 (1), pp. 127-37. - Publication Year :
- 2000
-
Abstract
- 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.
- Subjects :
- Amino Acid Motifs
Amino Acid Sequence
Animals
Binding Sites
COS Cells
Estrogen Receptor alpha
Humans
In Vitro Techniques
Ligands
Molecular Sequence Data
Phosphorylation
Protein Structure, Quaternary
Protein Structure, Tertiary
Receptors, Estrogen chemistry
Receptors, Estrogen genetics
Recombinant Proteins chemistry
Recombinant Proteins genetics
Recombinant Proteins metabolism
Serine metabolism
Transcription Factor TFIIH
Transcription Factors chemistry
Transcription Factors genetics
Transcriptional Activation
Cyclin-Dependent Kinase-Activating Kinase
Cyclin-Dependent Kinases
Protein Serine-Threonine Kinases metabolism
Receptors, Estrogen metabolism
Transcription Factors metabolism
Transcription Factors, TFII
Subjects
Details
- Language :
- English
- ISSN :
- 1097-2765
- Volume :
- 6
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Molecular cell
- Publication Type :
- Academic Journal
- Accession number :
- 10949034