The interleukin-2 receptor (IL-2R) 1 chain (IL-2RPI) is an essential signaling component of high-and intermediate-affinity . Our laboratory previously reported that a DNA fragment containing 857 bp of 5'-flanking sequence of the human I,-2RI3 gene exhibited promoter activity. We have now further characterized the promoter and delineated cis-acting regulatory regions. The region downstream of -363 is critical for basal and phorbol myristate acetate-inducible IL-2R13 promoter activity and contains at least three enhancerlike regions. Among them, the -56 to -34 enhancer was the most potent and had high-level activity in two T-celi lines but not in nonlymphoid HeLaS3 and MG63 cells. This enhancer contains a GGAA Ets binding site which bound two Ets family proteins, Ets-1 and GA-binding protein in vitro. Mutation of the Ets motif strongly diminished both promoter and enhancer activities. We conclude that this Ets binding site plays a key role in regulating basal and phorbol myristate acetate-inducible IL-2R13 promoter activity and may also contribute to tissue-specific expression of the IL-2R13 gene.
Antigen stimulation of T cells results in production of interleukin-2 (IL-2) and induction of high-affinity IL-2 receptor (IL-2R). The interaction of IL-2 with high-affinity IL-2Rinduces signals which result in T-cell proliferation (reviewed in references 25, 39, and 48). High-and/or intermediateaffinity IL-2Rs also play important roles in IL-2-induced cytolytic activity of T cells (38), natural killer cells (38,46), and neutrophils (9, 50) and in immunoglobulin production by B cells (29,48). Since high-affinity receptors contain a (26, 30), 1 (18,35,42,47), and -y (40, 41) chains, and intermediate-affinity receptors contain 13 and y chains, IL-2RP is an essential subunit of both classes of functional receptors.