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Science 14 June 1991: Vol. 252. no. 5012, pp. 1523 - 1528 DOI: 10.1126/science.2047859
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Articles
Science, Vol 252, Issue 5012, 1523-1528
Copyright © 1991 by American Association for the Advancement of Science
Interaction of the IL-2 receptor with the src-family kinase p56lck: identification of novel intermolecular association
M Hatakeyama,
T Kono,
N Kobayashi,
A Kawahara,
SD Levin,
RM Perlmutter,
and
T Taniguchi
Institute for Molecular and Cellular Biology, Osaka University, Japan.
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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- Interleukin-2 Carbohydrate Recognition Modulates CTLL-2 Cell Proliferation.
- K. Fukushima and K. Yamashita (2001)
J. Biol. Chem.
276, 7351-7356
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