Interaction of the IL-2 receptor with the src-family kinase p56lck: identification of novel intermolecular association |
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Authors: | M Hatakeyama T Kono N Kobayashi A Kawahara S D Levin R M Perlmutter T Taniguchi |
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Institution: | Institute for Molecular and Cellular Biology, Osaka University, Japan. |
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Abstract: | In the interleukin-2 (IL-2) system, intracellular signal transduction is triggered by the beta chain of the IL-2 receptor (IL-2R beta); however, the responsible signaling mechanism remains unidentified. Evidence for the formation of a stable complex of IL-2R beta and the lymphocyte-specific protein tyrosine kinase p56lck is presented. Specific association sites were identified in the tyrosine kinase catalytic domain of p56lck and in the cytoplasmic domain of IL-2R beta. As a result of interaction, IL-2R beta became phosphorylated in vitro by p56lck. Treatment of T lymphocytes with IL-2 promotes p56lck kinase activity. These data suggest the participation of p56lck as a critical signaling molecule downstream of IL-2R via a novel interaction. |
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