• Register
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.


Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.


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


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


Molecular endocrinology (Baltimore, Md.)

Publication Data

November 30, 1999

Associated Grants


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