Thrombopoietin (TPO) induces tyrosine phosphorylation and activation of STAT5 and STAT3

Chris M. Bacon, P. Justin Tortolani, Akihiro Shimosaka, Robert C. Rees, Dan L. Longo, John J. O'Shea

Research output: Contribution to journalArticle

Abstract

The growth and differentiation of megakaryocytes are regulated by thrombopoietin (TPO), a recently characterized cytokine which exerts its effects via a member of the hematopoietin receptor superfamily, c-Mpl. Since many cytokines which bind hematopoietin receptors activate the STAT family of transcription factors, we investigated whether STAT proteins were activated by TPO. TPO induced the formation of a DNA-binding complex recognizing a known STAT binding sequence. STAT5 was a major component of this DNA-binding complex, and STAT5 was tyrosine phosphorylated in response to TPO. Additionally, TPO-induced the tyrosine phosphorylation and DNA-binding activity of STAT3. Together with the recent demonstration of JAK2 activation in response to TPO, the data presented here define a rapid signaling pathway likely to be important in TPO-induced gene regulation.

Original languageEnglish (US)
Pages (from-to)63-68
Number of pages6
JournalFEBS Letters
Volume370
Issue number1-2
DOIs
StatePublished - Aug 14 1995
Externally publishedYes

Keywords

  • Signal transducers and activators of transcription (STAT)
  • Signal transduction
  • Thrombopoietin
  • Tyrosine phosphorylation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Thrombopoietin (TPO) induces tyrosine phosphorylation and activation of STAT5 and STAT3'. Together they form a unique fingerprint.

Cite this