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Activates Stat6 and Leads to the Formation of Stat2:Stat6 Complexes in B Cells1
Department of Medicine, Columbia University, New York, NY 10032
IFN-
consists of a family of highly homologous proteins, which
exert pleiotropic effects on a wide variety of cell types. The biologic
activities of IFN- are mediated by its binding to a multicomponent
receptor complex resulting in the activation of the Janus kinase-STAT
signaling pathway. In most cell types, activation of Stat1 and Stat2 by
IFN- leads to the formation of either STAT homo-/heterodimers or of
the IFN-stimulated gene factor 3 complex composed of Stat1, Stat2, and
p48, a non-STAT protein. These distinct transcriptional complexes then
target two different sets of cis-elements, 
-activated
sites and IFN-stimulated response elements. Here, we report that
IFN- can activate complexes containing Stat6, which, until now, has
been primarily associated with signaling by two cytokines with biologic
overlap, IL-4 and IL-13. Induction of Stat6 complexes by IFN-
appears to be cell type specific, given that tyrosine phosphorylation
of Stat6 in response to IFN- is predominantly detected in B cells.
Activation of Stat6 by IFN- in B cells is accompanied by the
formation of novel Stat2:Stat6 complexes, including an IFN-stimulated
gene factor 3-like complex containing Stat2, Stat6, and p48. B cell
lines resistant to the antiproliferative effects of IFN- display a
decrease in the IFN--mediated activation of Stat6. Activation of
Stat6 as well as of Stat2:Stat6 complexes by IFN- in B cells may
allow modulation of target genes in a cell type-specific
manner.
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