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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.

Abstract : 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.
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https://hal-univ-tours.archives-ouvertes.fr/hal-02427581
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Submitted on : Friday, January 3, 2020 - 5:38:54 PM
Last modification on : Tuesday, January 14, 2020 - 1:56:02 PM

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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 , National Academy of Sciences, 1995, 92 (12), pp.5482-5486. ⟨10.1073/pnas.92.12.5482⟩. ⟨hal-02427581⟩

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