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.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
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).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
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
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/370151a0
- Springer Nature Limited
This article is cited by
-
Does baricitinib reduce disease activity in patients with systemic lupus erythematosus? A systematic review and meta-analysis of randomized controlled trials
Clinical Rheumatology (2024)
-
Scope of JAK Inhibitors in Children: Recent Evidence and Way Forward
Pediatric Drugs (2023)
-
Janus kinase-targeting therapies in rheumatology: a mechanisms-based approach
Nature Reviews Rheumatology (2022)
-
Endothelial Jak3 expression enhances pro-hematopoietic angiocrine function in mice
Communications Biology (2021)
-
JAK–STAT pathway targeting for the treatment of inflammatory bowel disease
Nature Reviews Gastroenterology & Hepatology (2020)