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Science 5 May 1989:
Vol. 244. no. 4904, pp. 551 - 556
DOI: 10.1126/science.2785715
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Articles

Science, Vol 244, Issue 4904, 551-556
Copyright © 1989 by American Association for the Advancement of Science

articles

Interleukin-2 receptor beta chain gene: generation of three receptor forms by cloned human alpha and beta chain cDNA's

M Hatakeyama, M Tsudo, S Minamoto, T Kono, T Doi, T Miyata, M Miyasaka, and T Taniguchi

Institute for Molecular and Cellular Biology, Osaka University, Japan.

Interleukin-2 (IL-2) binds to two distinct receptor molecules, the IL-2 receptor alpha (IL-2R alpha, p55) chain and the newly identified IL-2 receptor beta (IL-2R beta, p70-75) chain. The cDNA encoding the human IL-2R beta chain has now been isolated. The overall primary structure of the IL-2R beta chain shows no apparent homology to other known receptors. Unlike the IL-2R alpha chain, the IL-2R beta chain has a large cytoplasmic region in which a functional domain (or domains) mediating an intracellular signal transduction pathway (or pathways) may be embodied. The cDNA-encoded beta chain binds and internalizes IL-2 when expressed on T lymphoid cells but not fibroblast cells. Furthermore, the cDNA gives rise to the generation of high-affinity IL-2 receptor when co-expressed with the IL-2R alpha chain cDNA.


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