NF-kappaB subunit regulation in non-transformed CD4+ T lymphocytes

Regulation of interleukin-2 (IL-2) gene expression by the p50 and p65 subunits of the DNA binding protein NF-κB was studied in nontransformed CD4⁺ T lymphocyte clones. A homodimeric complex of the NF-κB p50 subunit was found in resting T cells. The amount of p50-p50 complex decreased after full antigenic stimulation, whereas the amount of the NF-κB p50-p65 heterodimer was increased. Increased expression of the IL-2 gene and activity of the IL-2 κB DNA binding site correlated with a decrease in the p50-p50 complex Overexpression of p50 repressed IL-2 promoter expression. The switch from p50-p50 to p50-p65 complexes depended on a protein that caused sequestration of the p50-p50 complex in the nucleus.