Serine phosphorylation of STATs

Oncogene. 2000 May 15;19(21):2628-37. doi: 10.1038/sj.onc.1203481.


Tyrosine phosphorylation regulates the dimerization of STATs as an essential prerequisite for the establishment of a classical JAK-STAT signaling path. However, most vertebrate STATs contain a second phosphorylation site within their C-termini. The phosphorylated residue in this case is a serine contained within a P(M)SP motif, and in the majority of situations its mutation to alanine alters transcription factor activity. This review addresses recent advances in understanding the regulation of STAT serine phosphorylation, as well as the kinases and other signal transducers implied in this process. The biochemical and biological consequences of STAT serine phosphorylation are discussed. Oncogene (2000).

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Nucleus / metabolism
  • Conserved Sequence
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism*
  • Humans
  • MAP Kinase Signaling System
  • Molecular Sequence Data
  • Phosphorylation
  • Phosphoserine / metabolism*
  • Phosphotyrosine / metabolism
  • STAT1 Transcription Factor
  • Trans-Activators / chemistry
  • Trans-Activators / metabolism*
  • Transcriptional Activation


  • DNA-Binding Proteins
  • STAT1 Transcription Factor
  • STAT1 protein, human
  • Trans-Activators
  • Phosphoserine
  • Phosphotyrosine