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      Cytoplasmic domains of the interleukin-2 receptor beta and gamma chains mediate the signal for T-cell proliferation.

      Nature

      metabolism, Tyrosine, physiology, T-Lymphocytes, Stem Cell Factor, immunology, Signal Transduction, Recombinant Fusion Proteins, chemistry, Receptors, Interleukin-2, Receptors, Colony-Stimulating Factor, Receptor Protein-Tyrosine Kinases, Proto-Oncogene Proteins c-kit, Proto-Oncogene Proteins, Phosphorylation, Molecular Sequence Data, Mice, Lymphocyte Activation, Humans, Hematopoietic Cell Growth Factors, Granulocyte-Macrophage Colony-Stimulating Factor, Cell Line, Biopolymers, Base Sequence, B-Lymphocytes, Animals

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          Abstract

          The interleukin-2 receptor (IL-2R) consists of three distinct chains (alpha, beta, gamma) which bind IL-2 and generate a proliferative signal in T cells. To define the mechanism of receptor activation, chimaeric receptors were constructed from the intracellular region of either IL-2R beta or IL-2R gamma and the extracellular region of c-kit, a receptor tyrosine kinase that homodimerizes on binding stem cell factor (SCF). We report here that binding of SCF to the beta-chain chimaera induced proliferation of the pro-B-cell line BA/F3, but not T cells. But in T cells expressing both the beta- and gamma-chain chimaeras, SCF induced proliferation and tyrosine phosphorylation characteristic of the native IL-2R signal. Chimaeric IL-2 receptor beta and gamma chains constructed with the heterodimeric extracellular regions of the granulocyte-macrophage colony stimulating factor receptor (GM-CSFR) also provided the IL-2R signal. Thus, heterodimerization of the cytoplasmic domains of IL-2R beta and -gamma appears necessary and sufficient for signalling in T cells.

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          Journal
          10.1038/369333a0
          7514277

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