Abstract
The nuclear factor of activated T cells (NFAT) group of transcription factors regulates gene expression in immune and non-immune cells. NFAT-mediated gene transcription is orchestrated, in part, by formation of a composite regulatory element. Here we demonstrate that NFAT interacts with transcription factor CCAAT/enhancer-binding protein (C/EBP) to form a composite enhancer complex, to potentiate expression of the peroxisome proliferator-activated receptor-gamma2 gene. Formation of a ternary NFAT.C/EBP.DNA complex is required for the transcriptional cooperation. A similar NFAT.C/EBP composite element is found in the regulatory region of the insulin-like growth factor 2, angiotensin-converting enzyme homolog, and transcription factor POU4F3 genes. Thus, the NFAT.C/EBP composite element represents a novel regulatory enhancer to direct NFAT-mediated gene transcription.
Highlights
nuclear factor of activated T cells (NFAT) interacts with transcription factor AP-1 (Fos and Jun proteins) to form a cooperative composite enhancer (NFAT1⁄7AP-1) and to regulate expression of many cytokine genes [11]
We demonstrate that NFAT interacts with transcription factor CCAAT/enhancer-binding protein (C/EBP) to form a composite enhancer complex, to potentiate expression of the peroxisome proliferator-activated receptor-␥2 gene
We tested whether NFAT cooperates with C/EBP to regulate the peroxisome proliferator-activated receptor-␥2 (PPAR␥2) gene expression
Summary
NFAT interacts with transcription factor AP-1 (Fos and Jun proteins) to form a cooperative composite enhancer (NFAT1⁄7AP-1) and to regulate expression of many cytokine genes [11]. Identification of proteins that bind to DNase I-hypersensitive sites is important to understand transcriptional regulation. The PPAR␥2 distal NFAT element is located between the DHS1 and the DHS2 DNase I-hypersensitive site. The PPAR␥2-proximal NFAT element is located within DHS1 The proximity of these NFAT elements to the DNase I-hypersensitive sites suggests that understanding the molecular basis of NFAT-mediated transcription will shed new light on the regulation of PPAR␥2 gene. The transcription cooperation is mediated, in part, by the formation of a composite NFAT1⁄7C/EBP complex on the PPAR␥2-proximal NFAT element. The NFAT1⁄7C/EBP complex represents a novel composite regulatory element to direct NFAT-mediated gene expression
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