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IL-2 Signaling Involves Recruitment and Activation of Multiple Protein Tyrosine Kinases by the IL-2 Receptor

The IL-2 receptor (IL-2R) consists of three subunits, the IL-2R alpha, IL-2R beta, and IL-2R gamma chains, the last of which is also used in the receptors for IL-4, IL-7, IL-9, IL-13, and IL-15. The IL-2-induced proliferative signals emanate from the cytoplasmic domains of IL-2R beta and IL-2R gamma...

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Bibliographic Details
Published in:Annals of the New York Academy of Sciences 1995-09, Vol.766 (1), p.235-244
Main Authors: TANIGUCHI, TADATSUGU, MIYAZAKI, TADAAKI, MINAMI, YASUHIRO, KAWAHARA, ATSUO, FUJII, HODAKA, NAKAGAWA, YOKO, HATAKEYAMA, MASANORI, LIU, ZHAO-JUN
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Language:English
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Summary:The IL-2 receptor (IL-2R) consists of three subunits, the IL-2R alpha, IL-2R beta, and IL-2R gamma chains, the last of which is also used in the receptors for IL-4, IL-7, IL-9, IL-13, and IL-15. The IL-2-induced proliferative signals emanate from the cytoplasmic domains of IL-2R beta and IL-2R gamma, but the nature and function of the signaling molecules that transmit these signals are not fully understood. Here we summarize our current understanding of the mechanisms by which IL-2R transmit signals by using multiple protein kinases. In fact, at least four protein tyrosine kinases (PTKs) are physically associated with IL-2R: p56lck (and its members), Syk PTK, and the Janus kinases, Jak1 and Jak3. cDNA expression studies revealed that the activation of these PTKs is critical for IL-2-induced proliferative signal transmission. Our findings indicate that a unique property of the IL-2R cytoplasmic domains is to recruit a variety of signaling molecules, which may suggest a mechanism by which these PTKs and other signaling molecules function in concert.
ISSN:0077-8923
1749-6632
DOI:10.1111/j.1749-6632.1995.tb26671.x