NF-κB Subunit Regulation in Nontransformed CD4$^+$ T Lymphocytes

• Published in: Science (American Association for the Advancement of Science) 1992-06, Vol.256 (5062), p.1452-1456
• Main Authors: Kang, Sang-Mo, Tran, Annie-Chen, Grilli, Mariagrazia, Lenardo, Michael J.
• Format: Article
• Language: English
• Subjects: Animals; Antigens; Base Sequence; Binding Sites; CD4 Antigens - immunology; Cell Line; Cell Nucleus - physiology; Cell separation; Chloramphenicol O-Acetyltransferase - genetics; Chloramphenicol O-Acetyltransferase - metabolism; Clone Cells; Columbidae; DNA; DNA - genetics; Gene expression; Gene Expression Regulation; Interleukin-2 - genetics; Macromolecular Substances; Messenger RNA; Mice; Molecular Sequence Data; NF-kappa B - metabolism; Oligonucleotide Probes; Oligonucleotides; Promoter Regions, Genetic; Recombinant Fusion Proteins - metabolism; RNA, Messenger - metabolism; T lymphocytes; T-Lymphocyte Subsets - immunology; Transfection; Tumor Necrosis Factor-alpha - pharmacology
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.1604322

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-κ B$ 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.