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Volume 272, Number 8, Issue of February 21, 1997 pp. 4993-4999
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Chimeric Erythropoietin-Interferon gamma  Receptors Reveal Differences in Functional Architecture of Intracellular Domains for Signal Transduction

(Received for publication, September 24, 1996, and in revised form, December 9, 1996)

Geetha Muthukumaran , Serguei Kotenko , Robert Donnelly , James N. Ihle Dagger and Sidney Pestka

From the Department of Molecular Genetics and Microbiology, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854-5635 and the Dagger  Department of Biochemistry, St. Jude Children's Hospital, Memphis, Tennessee 38105

Binding of interferon gamma (IFN-gamma ) causes oligomerization of the two interferon gamma  receptor (IFN-gamma R) subunits, receptor chain 1 (IFN-gamma R1, the ligand-binding chain) and the second chain of the receptor (IFN-gamma R2), and causes activation of two Jak kinases (Jak1 and Jak2). In contrast, the erythropoietin receptor (EpoR) requires only one receptor chain and one Jak kinase (Jak2). Chimeras between the EpoR and the IFN-gamma R1 and IFN-gamma R2 chains demonstrate that the architecture of the EpoR and the IFN-gamma R complexes differ significantly. Although IFN-gamma R1 alone cannot initiate signal transduction, the chimera EpoR/gamma R1 (extracellular/intracellular) generates slight responses characteristic of IFN-gamma in response to Epo and the EpoR/gamma R1·EpoR/gamma R2 heterodimer is a fully functional receptor complex. The results demonstrate that the configuration of the extracellular domains influences the architecture of the intracellular domains.


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Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.