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Science 19 January 1990:
Vol. 247. no. 4940, pp. 324 - 327
DOI: 10.1126/science.2404337
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Articles

Science, Vol 247, Issue 4940, 324-327
Copyright © 1990 by American Association for the Advancement of Science

articles

Cloning of an interleukin-3 receptor gene: a member of a distinct receptor gene family

N Itoh, S Yonehara, J Schreurs, DM Gorman, K Maruyama, A Ishii, I Yahara, K Arai, and A Miyajima

Department of Molecular Biology, DNAX Research Institute of Molecular and Cellular Biology, Palo Alto, CA 94304.

Interleukin-3 (IL-3) binds to its receptor with high and low affinities, induces tyrosine phosphorylation, and promotes the proliferation and differentiation of hematopoietic cells. A binding component of the IL-3 receptor was cloned. Fibroblasts transfected with the complementary DNA bound IL-3 with a low affinity [dissociation constant (Kd) of 17.9 +/- 3.6 nM]. No consensus sequence for a tyrosine kinase was present in the cytoplasmic domain. Thus, additional components are required for a functional high affinity IL-3 receptor. A sequence comparison of the IL-3 receptor with other cytokine receptors (erythropoietin, IL-4, IL-6, and the beta chain IL-2 receptor) revealed a common motif of a distinct receptor gene family.


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