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JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin.

Erythropoietin (EPO) regulates the proliferation and differentiation of erythroid cells through interaction with its receptor (EPOR). Although EPOR is a member of the cytokine receptor superfamily and lacks a kinase domain, EPO induces tyrosine phosphorylation, which is correlated with gene transcription and mitogenesis. Here we demonstrate that EPO induces tyrosine phosphorylation of JAK2 kinase and activates its in vitro autophosphorylation. Using EPOR mutants, phosphorylation and activation of kinase activity correlate with the induction of mitogenesis. Furthermore, JAK2 physically associates with a membrane-proximal region of the EPOR cytoplasmic domain that is required for biological activity. The results support the hypothesis that JAK2 is the kinase that couples EPO binding to tyrosine phosphorylation and mitogenesis.

Pubmed ID: 8343951


  • Witthuhn BA
  • Quelle FW
  • Silvennoinen O
  • Yi T
  • Tang B
  • Miura O
  • Ihle JN



Publication Data

July 30, 1993

Associated Grants

  • Agency: NCI NIH HHS, Id: P30 CA21765
  • Agency: NIDDK NIH HHS, Id: R01 DK42932

Mesh Terms

  • 3T3 Cells
  • Animals
  • Cell Division
  • Enzyme Activation
  • Erythropoietin
  • Janus Kinase 2
  • Mice
  • Models, Biological
  • Phosphorylation
  • Protein-Tyrosine Kinases
  • Proto-Oncogene Proteins
  • Receptors, Erythropoietin
  • Recombinant Fusion Proteins
  • Signal Transduction
  • Transfection
  • Tyrosine