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(Received for publication, February
27, 1995; and in revised form, May 11, 1995) From the Interferon
Volume 270,
Number 29,
Issue of July 21, pp. 17528-17534, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
and
(Accessory Factor)
Chains of the Interferon
Receptor to Form a Functional Receptor
Unit Capable of Activating STAT Transcription Factors
(IFN
) induces the expression of early
response genes by tyrosine phosphorylation of Jak kinases and
transcription factors referred to as STAT proteins. The topology of the
IFN
receptor is partially understood and the relationship between
the
chain that binds the ligand and the 
chain that is
required for signal transduction is undefined. In a cell line which
expresses only the human chain, we show that these cells did not
activate Jak kinases or STAT proteins with human IFN, even though
Jak1 co-immunoprecipitated with the
chain. In cells unexposed to
IFN, Jak1 preferentially associated with the
chain, while
Jak2 associated with the chain. There was evidence for Jak1
kinase activity in untreated cells. For Jak2, kinase activity was
IFN-dependent. Although the
chain was
tyrosine-phosphorylated in response to ligand, we found no evidence for
tyrosine phosphorylation of the chain. These data are consistent
with a model of the IFN receptor in which Jak1 associates with the
chain, whereas Jak2 associates with the chain. IFN
clusters at least two receptor units which results in the tyrosine
phosphorylation of Jak1 and Jak2, the activation of Jak2 kinase
activity, and the recruitment of STAT1
resulting in its activation
by tyrosine phosphorylation.
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