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

Nucleic Acids Res. 1997 Jun 1;25(11):2062-7. doi: 10.1093/nar/25.11.2062.


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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Binding Sites
  • COS Cells
  • DNA / metabolism*
  • DNA-Binding Proteins / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Phosphorylation
  • STAT1 Transcription Factor
  • STAT3 Transcription Factor
  • Serine / metabolism*
  • Trans-Activators / metabolism*


  • DNA-Binding Proteins
  • STAT1 Transcription Factor
  • STAT3 Transcription Factor
  • Trans-Activators
  • Serine
  • DNA