Sk. Lee et al., STEROID-RECEPTOR COACTIVATOR-1 COACTIVATES ACTIVATING PROTEIN-1-MEDIATED TRANSACTIVATIONS THROUGH INTERACTION WITH THE C-JUN AND C-FOS SUBUNITS, The Journal of biological chemistry, 273(27), 1998, pp. 16651-16654
Steroid receptor coactivator-l (SRC-1) specifically bound to the trans
cription factor AP-I 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 su
bregion of SRC-1 (amino acids 1101-1441) that encompasses the previous
ly described histone acetyltransferase and receptor-binding domains. I
n mammalian cells, SRC-I, similar to the previous results with CBP-p30
0 (Arias, J., Alberts, A. S., Brindle, P., Claret, F. X., Smeal, T., K
arin, M., Feramisco, J., and Montminy, M. (1994) Nature 370, 226-229;
Bannister, A. J., and Kouzarides, T. (1995) EMBO J. 14, 4758-4762), po
tentiated the AP-l-mediated transactivations in a dose-dependent manne
r and derepressed the mutual inhibitions between nuclear receptors and
AP-1. Furthermore, coexpression of p300 further enhanced this SRC-1-p
otentiated level of transactivations. Thus, we concluded that at least
two distinct coactivator molecules may cooperate to regulate AP-l-dep
endent transactivations and mediate transrepression between AP-I and n
uclear receptors in vivo.