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J Biol Chem, Vol. 273, Issue 45, 29291-29294, November 6, 1998
B Signaling by CREB-binding Protein and Steroid Receptor
Coactivator-1
,,,
From the The p65 (RelA) component of nuclear factor- Vascular Research Division, Department of
Pathology, Brigham and Women's Hospital, and Harvard Medical School,
Boston, Massachusetts 02115, the § Department of
Biochemistry and Molecular Biophysics, Columbia University, New York,
New York 10032, the ¶ Department of Cellular and Molecular
Medicine, School and Department of Medicine, University of California,
San Diego, California 92093, §§ Howard Hughes Medical
Institute, University of California at San Diego, La Jolla, California
92093 and ** Genentech, Inc., South San Francisco, California 94080
B
(NF-B) and the glucocorticoid receptor (GR) mutually repress each
other's ability to activate transcription. Both of these
transcriptional activators depend upon the coactivators CREB-binding
protein (CBP) and steroid receptor coactivator-1 (SRC-1) for maximal
activity. Here we show that increased levels of CBP relieves the
inhibition of glucocorticoid-mediated repression of NF-B activity
and the NF-B-mediated repression of GR activity. SRC-1 can relieve
the NF-B-mediated repression of GR activity. We propose that
cross-talk between the p65 component of NF-B and glucocorticoid
receptors is due, at least in part, to nuclear competition for limiting
amounts of the coactivators CBP and SRC-1, thus providing a novel
mechanism for decreasing expression of genes involved in the
inflammatory response.
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