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*
Department of Immunology, Berlex Biosciences, Richmond CA 94804;
Department of Pharmacology, University of Illinois, Chicago, IL 60612; and
Institute of Theoretical and Experimental Biophysics, Russian Academy of Science, Pushchino, Moscow Region, Russia
The cytoplasmic domain of the human type I IFN receptor chain 2
(IFNAR2c or IFN-
RßL) was used as bait in a yeast two-hybrid system
to identify novel proteins interacting with this region of the
receptor. We report here a specific interaction between the cytoplasmic
domain of IFN-RßL and a previously identified protein, RACK-1
(receptor for activated C kinase). Using GST fusion proteins encoding
different regions of the cytoplasmic domain of IFN-RßL, the
minimum site for RACK-1 binding was mapped to aa 300–346. RACK-1
binding to IFN-RßL did not require the first 91 aa of RACK-1,
which includes two WD domains, WD1 and WD2. The interaction between
RACK-1 and IFN-RßL, but not the human IFN receptor chain 1 (IFNAR1
or IFN-R), was also detected in human Daudi cells by
coimmunoprecipitation. RACK-1 was shown to be constitutively associated
with IFN-RßL, and this association was not effected by stimulation
of Daudi cells with type I IFNs (IFN-ß1b). RACK-1 itself did not
become tyrosine phosphorylated upon stimulation of Daudi cells with
IFN-ß1b. However, stimulation of cells with either IFN-ß1b or PMA
did result in an increase in detectable immunofluorescence and
intracellular redistribution of RACK-1.
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