Interaction of the IL-2 Receptor with the src -Family Kinase p56 lck : Identification of Novel Intermolecular Association
- 14 June 1991
- journal article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 252 (5012), 1523-1528
- https://doi.org/10.1126/science.2047859
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.Keywords
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