Nucleic Acids Research, Vol 25, Issue 11 2062-2067, Copyright © 1997 by Oxford University Press
Z Wen and JE Darnell Jr
During their polypeptide ligand-induced activation Stats (signaltransducers
andactivators oftranscription) 1 and 3 acquire, in addition to an
obligatory tyrosine phosphorylation, phosphorylation on serine which boosts
their transactivating potential [Wen, Z., Zhong, Z. and Darnell, J. E. Jr.
(1995) Cell 82, 241-250]. By examining phosphopeptide maps of wild-type and
mutant protein we show here that the Stat3 serine phosphorylation, like the
Stat1 serine phosphorylation, occurs on a single residue, serine 727.
Neither the DNA binding of Stat1 nor Stat3 is demonstrably affected by the
presence or absence of the serine phosphorylation. Thus the earlier
demonstration that transcription is enhanced by the presence of the serine
727 residue likely occurs after DNA binding. These findings do not agree
with earlier claims of excess serine to tyrosine phosphorylation in
activated Stats 1 and 3 or to claims of more stable DNA binding of serine
phosphorylated Stat dimers.
ARTICLES
Mapping of Stat3 serine phosphorylation to a single residue (727) and evidence that serine phosphorylation has no influence on DNA binding of Stat1 and Stat3
Laboratory of Molecular Cell Biology, The Rockefeller University, New York, NY 10021, USA.
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