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Science 14 April 1995:
Vol. 268. no. 5208, pp. 251 - 255
DOI: 10.1126/science.7716517
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Articles

Science, Vol 268, Issue 5208, 251-255
Copyright © 1995 by American Association for the Advancement of Science

articles

Cytokine signaling through nonreceptor protein tyrosine kinases

T Taniguchi

Department of Immunology, Faculty of Medicine, University of Tokyo, Japan.

Cytokines are a family of soluble mediators of cell-to-cell communication that includes interleukins, interferons, and colony-stimulating factors. The characteristic features of cytokines lie in their functional redundancy and pleiotropy. Most of the cytokine receptors that constitute distinct superfamilies do not possess intrinsic protein tyrosine kinase (PTK) domains, yet receptor stimulation usually invokes rapid tyrosine phosphorylation of intracellular proteins, including the receptors themselves. It is now clear that these receptors are capable of recruiting or activating (or both) a variety of nonreceptor PTKs to induce downstream signaling pathways. Thus, the intracytoplasmic structure of cytokine receptors has evolved so as to allow the combined action of different PTK family members expressed in different cell types, which may ultimately determine the activity of cytokines.


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   Abstract »    Full Text »    PDF »
Macrophage-Derived Nitric Oxide Regulates T Cell Activation via Reversible Disruption of the Jak3/STAT5 Signaling Pathway.
R. M. Bingisser, P. A. Tilbrook, P. G. Holt, and U. R. Kees (1998)
J. Immunol. 160, 5729-5734
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IL-6 Produced by Kupffer Cells Induces STAT Protein Activation in Hepatocytes Early During the Course of Systemic Listerial Infections.
S. H. Gregory, E. J. Wing, K. L. Danowski, N. van Rooijen, K. F. Dyer, and D. J. Tweardy (1998)
J. Immunol. 160, 6056-6061
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Prolactin (PRL) and Its Receptor: Actions, Signal Transduction Pathways and Phenotypes Observed in PRL Receptor Knockout Mice.
C. Bole-Feysot, V. Goffin, M. Edery, N. Binart, and P. A. Kelly (1998)
Endocr. Rev. 19, 225-268
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Human and Simian T-Cell Leukemia Viruses Type 2 (HTLV-2 and STLV-2pan-p) Transform T Cells Independently of Jak/STAT Activation.
J. C. Mulloy, T.-S. Migone, T. M. Ross, N. Ton, P. L. Green, W. J. Leonard, and G. Franchini (1998)
J. Virol. 72, 4408-4412
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Delineation of the Regions of Interleukin-2 (IL-2) Receptor beta  Chain Important for Association of Jak1 and Jak3. Jak1-INDEPENDENT FUNCTIONAL RECRUITMENT OF Jak3 TO IL-2Rbeta.
M.-h. Zhu, J. A. Berry, S. M. Russell, and W. J. Leonard (1998)
J. Biol. Chem. 273, 10719-10725
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Prolonged STAT1 Activation Related to the Growth Arrest of Malignant Lymphoma Cells by Interferon-alpha.
P. M. Grimley, H. Fang, H. Rui, E. F. Petricoin III, S. Ray, F. Dong, K. H. Fields, R. Hu, K. C. Zoon, S. Audet, et al. (1998)
Blood 91, 3017-3027
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Effect of tyrosine kinase inhibition on surfactant protein A gene expression during human lung development.
J. M. Klein, L. J. Dewild, and T. A. McCarthy (1998)
Am J Physiol Lung Cell Mol Physiol 274, L542-L551
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JAK2 and JAK1 Constitutively Associate With an Interleukin-5 (IL-5) Receptor alpha  and beta c Subunit, Respectively, and Are Activated Upon IL-5 Stimulation.
N. Ogata, T. Kouro, A. Yamada, M. Koike, N. Hanai, T. Ishikawa, and K. Takatsu (1998)
Blood 91, 2264-2271
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