Nuclear factor of activated T cells (NFAT)-dependent transactivation regulated by the coactivators p300/CREB-binding protein (CBP).
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.
Mesh Terms:
Acetyltransferases, Adenovirus E1A Proteins, CREB-Binding Protein, Cell Cycle Proteins, Cytokines, DNA-Binding Proteins, Histone Acetyltransferases, NFATC Transcription Factors, Nuclear Proteins, Precipitin Tests, Protein Binding, Saccharomyces cerevisiae Proteins, Subcellular Fractions, T-Lymphocytes, Trans-Activators, Transcription Factors, Transcriptional Activation, p300-CBP Transcription Factors
Acetyltransferases, Adenovirus E1A Proteins, CREB-Binding Protein, Cell Cycle Proteins, Cytokines, DNA-Binding Proteins, Histone Acetyltransferases, NFATC Transcription Factors, Nuclear Proteins, Precipitin Tests, Protein Binding, Saccharomyces cerevisiae Proteins, Subcellular Fractions, T-Lymphocytes, Trans-Activators, Transcription Factors, Transcriptional Activation, p300-CBP Transcription Factors
J. Exp. Med.
Date: Jun. 15, 1998
PubMed ID: 9625762
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