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Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892
The IL-4R induces proliferation and gene expression through the use
of conserved tyrosine residues located in growth and gene regulation
domains, respectively. We demonstrate that residues surrounding these
conserved tyrosines (juxtatyrosine residues) are essential for the
proper activation of the signaling molecules IRS-2 and Stat6, as well
as for IL-4-induced gene expression. Further, we found that the IL-4R
gene regulation domain (amino acids 557–657) contains a tyrosine-based
sequence (EAGYKAF) that can convey Stat6 DNA binding and gene
expression activities to a minimally active IL-4R mutant, 
557. Thus,
this tyrosine-based sequence can function as a mobile Stat6 activation
cassette. However, mutants bearing this sequence induced CD23
expression much less efficiently than did wild-type IL-4R, requiring
150-fold more IL-4 to reach maximal CD23 expression. Our results
indicate the importance of juxtatyrosine residues in IL-4R signaling
and argue for an essential role of extended domain structure in the
recognition and function of juxtatyrosine
sequences.
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