The Journal of Experimental Medicine
VeriKine-HS Human IFN-Beta
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© The Rockefeller University Press, 0022-1007/1998/6/2031/ $5.00
The Journal of Experimental Medicine, Volume 187, Number 12, June 15, 1998 2031-2036

Articles

Nuclear Factor of Activated T Cells (NFAT)-dependent Transactivation Regulated by the Coactivators p300/CREB-binding Protein (CBP)

Carmen García-Rodríguez and Anjana Rao

From the Department of Pathology, Harvard Medical School, and the Center for Blood Research, Boston, Massachusetts 02115

p300 and cAMP response element–binding protein (CREB)–binding protein (CBP) are members of a family of coactivators involved in the regulation of transcription and chromatin. We show that transcription factors of the nuclear factor of activated T cells (NFAT) family bind p300/CBP and recruit histone acetyltransferase activity from T cell nuclear extracts. The NH2-terminal transactivation domain of NFAT1 and the phospho-CREB- and E1A-binding sites of p300/CBP are involved in the interaction. The viral oncoprotein E1A inhibits NFAT-dependent transactivation in a p300-dependent manner. Recruitment of the coactivators p300/CBP by the transactivation domains of NFAT proteins is likely to play a critical role in NFAT-dependent gene expression during the immune response.

Key Words: transcriptional regulation • histone acetyltransferases • T cells • nuclear factor of activated T cells • cytokine gene expression

Address correspondence to Dr. Anjana Rao, Center for Blood Research, 200 Longwood Ave., Boston, MA 02115. Phone: 617-278-2360; Fax: 617-278-3280; E-mail: arao{at}cbr.med.harvard.edu

Abbreviations used: aa, amino acid(s); AP-1, activating protein-1; CBP, CREB-binding protein; CREB, cAMP response element–binding protein; DBD, DNA-binding domain; GST, glutathione S-transferase; HA, hemagglutinin; HAT, histone acetyltransferase; hGH, human growth hormone; Luc, luciferase; NFAT, nuclear factor of activated T cells.


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