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Steroid receptor coactivator-1 and its family members differentially regulate transactivation by the tumor suppressor protein p53.

The tumor suppressor protein p53 exerts its cell cycle-regulatory effects through its ability to function as a sequence-specific DNA-binding transcription factor. Herein, we show that p53 physically interacts with specific subregions of steroid receptor coactivator-1 (SRC-1) and its family members, p/CIP (p300/CBP interacting protein), xSRC-3, and AIB1 (amplified in breast cancer), originally isolated as transcription coactivators of nuclear receptors, as demonstrated by the yeast and mammalian two-hybrid tests as well as glutathione S-transferase pull-down assays. Interestingly, cotransfection of HeLa cells with SRC-1- or p/CIP expression vector potentiated the p53-mediated transactivation, whereas AIB1 and xSRC-3 were repressive. All of these SRC-1 members, however, similarly stimulated transactivation mediated by nuclear receptors and AP-1, as previously described. These results suggest that SRC-1 and its family members may differentially modulate the p53 transactivation in vivo.

Pubmed ID: 10551785

Authors

  • Lee SK
  • Kim HJ
  • Kim JW
  • Lee JW

Journal

Molecular endocrinology (Baltimore, Md.)

Publication Data

November 30, 1999

Associated Grants

None

Mesh Terms

  • Acetyltransferases
  • Bacterial Proteins
  • HeLa Cells
  • Histone Acetyltransferases
  • Humans
  • Nuclear Receptor Coactivator 1
  • Nuclear Receptor Coactivator 3
  • Oncogene Proteins
  • Protein Isoforms
  • Recombinant Proteins
  • Serine Endopeptidases
  • Trans-Activators
  • Transcription Factors
  • Transcriptional Activation
  • Transfection
  • Tumor Suppressor Protein p53