Steroid receptor coactivator-1 coactivates activating protein-1- mediated transactivations through interaction with the c-Jun and c-Fos subunits

Soo Kyung Lee, Han Jong Kim, Soon Young Na, Tae Sung Kim, Hueng Sik Choi, Suhn Young Im, Jae Woon Lee

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175 Scopus citations


Steroid receptor coactivator-1 (SRC-1) specifically bound to the transcription factor AP-1 subunits c-Jun and c-Fos, as demonstrated by the yeast two-hybrid tests and glutathione S-transferase pull down assays. The c- Jun and c-Fos binding sites were localized to the C-terminal subregion of SRC-1 (amino acids 1101-1441) that encompasses the previously described histone acetyltransferase and receptor-binding domains. In mammalian cells, SRC-1, similar to the previous results with CBP-p300 (Arias, J., Alberts, A. S., Brindle, P., Claret, F. X., Smeal, T., Karin, M., Feramisco, J., and Montminy, M. (1994) Nature 370, 226-229; Bannister, A. J., and Kouzarides, T. (1995) EMBO J. 14, 4758-4762), potentiated the AP-1-mediated transactivations in a dose-dependent manner and derepressed the mutual inhibitions between nuclear receptors and AP-1. Furthermore, coexpression of p300 further enhanced this SRC-1-potentiated level of transactivations. Thus, we concluded that at least two distinct coactivator molecules may cooperate to regulate AP-1-dependent transactivations and mediate transrepression between AP-1 and nuclear receptors in vivo.

Original languageEnglish (US)
Pages (from-to)16651-16654
Number of pages4
JournalJournal of Biological Chemistry
Issue number27
StatePublished - Jul 3 1998


ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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