Abstract
INTERLEUKIN-2 is an autocrine growth factor for T cells1,2 which also activates other cells including B cells3 and natural killer cells4. The subunits of the interleukin-2 receptor (IL-2R) lack intrinsic enzymatic activity, but protein tyrosine phosphorylation is a critical event following ligand binding and src family kinases, such as Lck, are known to be activated by IL-2 (refs 5–9). However, IL- 2 signalling can occur in the absence of receptor interaction with Lck, suggesting that other protein tyrosine kinases might be important10. Here we report that a new member of the Janus family of kinases (Jak-3) is coupled to the IL-2R in human peripheral blood T cells and natural killer cells.
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References
Taniguchi, T. & Minami, Y. Cell 73, 5–8 (1993).
Waldman, T. A. A. Rev. Biochem. 58, 875–911 (1989).
Waldman, T. A. et al. J. exp. Med. 160, 1450–1466 (1984).
Henry, C. S., Kwibayashi, K., Kern, D. E. & Gillis, S. Nature 291, 335–338 (1981).
Minami, Y., Kono, T., Miyazaki, T. & Taniguchi, T. A. Rev. Immun. 11, 245–267 (1993).
Mills, G. B. et al. J. biol. Chem. 265, 3561–3567 (1990).
Farrar, W. L. & Ferris, D. K. J. biol. chem. 264, 12562–12567 (1989).
Merida, I. & Gaulton, G. N. J. biol. Chem. 265, 5690–5694 (1990).
Hatakeyama, M. et al. Science 262, 1523–1528 (1991).
Hatakeyama, M., Mori, H., Doi, T. & Tanaguchi, T. Cell 59, 837–845 (1989).
Kawamura, M. et al. Proc. natn. Acad. Sci. U.S.A. (in the press).
Watling, D. et al. Nature 366, 166–170 (1993).
Velasquez, L., Fellows, M., Stark, G. R. & Pellegrini, S. Cell 70, 313–322 (1992).
Muller, M. et al. Nature 366, 129–135 (1993).
Taniguchi, T. A. Rev. Immun. 4, 69–96 (1988).
Leonard, W. J., Depper, J. M., Robb, R. J., Waldmann, T. A. & Greene, W. C. Proc. natn. Acad. Sci. U.S.A. 80, 6957–6961 (1983).
Stahl, N. et al. Science 263, 92–95 (1994).
Kirken, R. A., Rui, H., Evan, G. A. & Farrar, W. L. J. biol. Chem. 268, 22765–22770 (1993).
Argetsinger, L. S. et al. Cell 74, 237–244 (1993).
Silvennoinen, O., Ihle, J. N., Schlessinger, J. & Levy, O. E. Nature 366, 583–585 (1993).
Silvennoinen, O. et al. Proc. natn. Acad. Sci. U.S.A. 90, 8429–33 (1993).
Witthuhn, B. A. et al. Cell 74, 227–236 (1993).
Russell, S. M. et al. Science 262, 1880–1887 (1993).
Kondo, M. et al. Science 262, 1874–1877 (1993).
Kishimoto, T., Taga, T. & Akira, S. Cell 76, 253–262 (1994).
Stahl, N. & Yancopoulos, G. D. Cell 74, 587–590 (1993).
Pellegrini, S. & Schridler, C. Trends biochem. Sci. 18, 338–342 (1993).
Witthuhn, B. A. et al. Nature 370, 153–157 (1994).
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Johnston, J., Kawamura, M., Kirken, R. et al. Phosphorylation and activation of the Jak-3 Janus kinase in response to interleukin-2. Nature 370, 151–153 (1994). https://doi.org/10.1038/370151a0
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DOI: https://doi.org/10.1038/370151a0
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