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Repression of IL-2 Promoter Activity by the Novel Basic Leucine Zipper p21^SNFT Protein^{1 ,2}

Milena Iacobelli^*, William Wachsman and Kathleen L. McGuire^3,*

^* Department of Biology and Molecular Biology Institute, San Diego State University, San Diego, CA 92182; and Medical and Research Services, San Diego Veterans Affairs Medical Center, Division of Hematology/Oncology, and Cancer Center, University of California-San Diego, La Jolla, CA 92093

IL-2 is the major autocrine and paracrine growth factor produced by T cells upon T cell stimulation. The inducible expression of IL-2 is highly regulated by multiple transcription factors, particularly AP-1, which coordinately activate the promoter. Described here is the ability of the novel basic leucine zipper protein p21^SNFT to repress AP-1 activity and IL-2 transcription. A detailed analysis of the repression by p21^SNFT repression on the IL-2 promoter distal NF-AT/AP-1 site demonstrates that it can bind DNA with NF-AT and Jun, strongly suggesting that it represses NF-AT/AP-1 activity by competing with Fos proteins for Jun dimerization. The importance of this repression is that p21^SNFT inhibits the trans-activation potential of protein complexes that contain Jun, thereby demonstrating an additional level of control for the highly regulated, ubiquitous AP-1 transcription factor and the IL-2 gene.

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