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

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

Authors

  • Chen D
  • Riedl T
  • Washbrook E
  • Pace PE
  • Coombes RC
  • Egly JM
  • Ali S

Journal

Molecular cell

Publication Data

July 31, 2000

Associated Grants

None

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