JBC INTERFERin siRNA transfection reagent

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J Biol Chem, Vol. 273, Issue 6, 3144-3147, February 6, 1998

COMMUNICATION
Differential Use of the beta L Subunit of the Type I Interferon (IFN) Receptor Determines Signaling Specificity for IFNalpha 2 and IFNbeta

Paul DomanskiDagger , Owen W. NadeauDagger , Leonidas C. Platanias§, Eleanor Fish, Merrill Kellumpar , Paula Pithapar , and Oscar R. ColamoniciDagger

From the Dagger  Department of Pathology, University of Tennessee, Memphis, Tennessee 38163, the § Section of Hematology/Oncology, Department of Medicine, University of Illinois at Chicago and West Side Veterans Affairs Hospital, Chicago, Illinois 60607, the  Department of Medical Genetics and Microbiology, University of Toronto, Toronto, Ontario M5S 1A8, Canada, and the par  Oncology Center, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21231

The signaling specificity for cytokines that have common receptor subunits is achieved by the presence of additional cytokine-specific receptor components. In the type I interferon (IFN) family, all 14 subtypes of IFNalpha , IFNbeta , and IFNomega bind to the same alpha  and beta L subunits of the type I IFN-R, yet differences in signaling and biological effects exist among them. Our data demonstrate that IFNalpha 2 and IFNbeta utilize different regions of the beta L subunit for signaling. Thus, in contrast to other cytokine systems, signal diversity in the type I IFN system can be accomplished within the same receptor complex by utilizing different regions of the same receptor subunits.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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