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J Biol Chem, Vol. 273, Issue 28, 17634-17642, July 10, 1998
From Tularik Inc.,
South San Francisco, California 94080
The SH2 domain of the STAT family of
transcription factors is essential for STAT binding to phosphorylated
cytoplasmic domains of activated cytokine receptors. Furthermore, the
same domain mediates dimerization of activated STAT monomers, a
prerequisite for DNA binding by this family of proteins. To identify
amino acid residues within the STAT protein that mediate these various interactions, we have carried out an extensive mutational analysis of
the Stat6 SH2 domain. Recombinant proteins carrying C-terminal deletions or double alanine substitutions were expressed in mammalian and insect cells and assayed for DNA binding, transcription activation, tyrosine phosphorylation, and the ability to interact with a
tyrosine-phosphorylated peptide derived from the interleukin-4 receptor
signaling chain. From these studies, we have identified amino acids
that are required for both DNA binding and interleukin-4 receptor
interaction, as well as residues that when mutated impair only one of
the two functions. Our results suggest that the structural homology
between the SH2 domain of Stat6 and that of the distantly related Src protein may be higher than predicted on the basis of primary amino acid
sequence comparisons. However, the two types of SH2 domains may differ
at their C-terminal ends.
Mutational Analysis of the STAT6 SH2 Domain
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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