Regulation of Estrogen Receptor-Dependent Transcriptional Activation by a Cyclin-Dependent Kinase.

Abstract

The estrogen receptor a is transcription factor that is regulated by ligand binding and phosphorylation. The phosphorylation of three serine residues (S104, S106 and S118) located within the N-terminal transcriptional activation domain (AF- 1) of the receptor are important for full receptor transcriptional activation. We provide evidence that alteration in the regulation of cyclinA/Cdk2 complex lead to changes in hormone-dependent and hormone-independent transcriptional enhancement by ER This is accomplished, at least in part, through the direct phosphorylation of ER S104, S106 and S118 by the cyclinA/Cdk2 complex. Since alterations in cydin dependent kinase regulatory proteins are a common feature in breast cancer, these findings provide a framework for understanding the mechanism by which CDK dysregulation can directly affect ER signaling through alterations in receptor phosphorylation.

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Document Details

Document Type
Technical Report
Publication Date
Oct 01, 1998
Accession Number
ADA366903

Entities

People

  • Janet M. Trowbridge

Organizations

  • New York University

Tags

DTIC Thesaurus Topics

  • Amino Acids
  • Anti-Bacterial Agents
  • Biochemistry
  • Biotechnology
  • Breast Cancer
  • Calcium Compounds
  • Carcinoma
  • Cell Line
  • Cell Physiological Processes
  • Chemistry
  • Culture Media
  • Epithelial Cells
  • Estrogens
  • Hormones
  • Neoplasms
  • Phosphoamino Acids
  • Polymerase Chain Reaction

Fields of Study

  • Biology

Readers

  • Breast cancer cell signaling and growth regulation.
  • Molecular Biology and Genetics