Activation of Stat5 by interleukin 2 requires a carboxyl-terminal region of the interleukin 2 receptor beta chain but is not essential for the proliferative signal transmission.

H. Fujii , Y. Nakagawa , U. Schindler , A. Kawahara , H. Mori , F. Gouilleux (1) , B. Groner , J. Ihle , Y. Minami , T. Miyazaki (2)

1 GICC UMR 6239 CNRS - Génétique, immunothérapie, chimie et cancer (GICC), UMR 6239 CNRS [2008-2011]
2 RIKEN RNC - RIKEN Nishina Center for Accelerator-Based Science [Wako]

The high-affinity interleukin 2 (IL-2) receptor (IL-2R) consists of three subunits: the IL-2R alpha, IL-2R beta c, and IL-2R gamma c chains. Two members of the Janus kinase family, Jak1 and Jak3, are associated with IL-2R beta c and IL-2R gamma c, respectively, and they are activated upon IL-2 stimulation. The cytokine-mediated Jak kinase activation usually results in the activation of a family of latent transcription factors termed Stat (signal transducer and activator of transcription) proteins. Recently, the IL-2-induced Stat protein was purified from human lymphocytes and found to be the homologue of sheep Stat5/mammary gland factor. We demonstrate that the human Stat5 is activated by IL-2 and that Jak3 is required for the efficient activation. The cytoplasmic region of the IL-2R beta c chain required for activation of Stat5 is mapped within the carboxyl-terminal 147 amino acids. On the other hand, this region is not essential for IL-2-induced cell proliferation.

Domains: Life Sciences [q-bio]

H. Fujii, Y. Nakagawa, U. Schindler, A. Kawahara, H. Mori, et al.. Activation of Stat5 by interleukin 2 requires a carboxyl-terminal region of the interleukin 2 receptor beta chain but is not essential for the proliferative signal transmission.. Proceedings of the National Academy of Sciences of the United States of America, 1995, 92 (12), pp.5482-5486. ⟨10.1073/pnas.92.12.5482⟩. ⟨hal-02427581⟩