Transmembrane signaling of interleukin 2 receptor. Conformation and function of human interleukin 2 receptor (p55)/insulin receptor chimeric molecules.
Chimeric genes were constructed which gave rise to the expression of novel receptor molecules consisting of the extracellular domain of the human interleukin 2 receptor (IL-2-R; p55 or Tac antigen) joined to the transmembrane domain and either full-length or truncated cytoplasmic domain of the human insulin receptor (Ins-R). Expression studies using mouse T cell line EL-4 revealed that the chimeric receptors are able to manifest properties indistinguishable from the authentic IL-2-R. On the other hand, stimulation of the tyrosine kinase activity by IL-2 was not observed in the chimeric receptor with the entire cytoplasmic domain of the Ins-R. These findings thus shed light on the structural conformation and functioning of the IL-2-R complex.
D000818:Animals; D002460:Cell Line; D002462:Cell Membrane; D003593:Cytoplasm; D004247:DNA; D004274:DNA, Recombinant; D006801:Humans; D051379:Mice; D010766:Phosphorylation; D010957:Plasmids; D011494:Protein Kinases / Q000378:metabolism; D011972:Receptor, Insulin; D011971:Receptors, Immunologic / Q000502:physiology; D015375:Receptors, Interleukin-2
D004274:DNA, Recombinant; D011971:Receptors, Immunologic; D015375:Receptors, Interleukin-2; D004247:DNA; D011494:Protein Kinases; D011972:Receptor, Insulin