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Tyrosine kinase JAK1 is associated with the granulocyte-colony-stimulating factor receptor and both become tyrosine-phosphorylated after receptor activation.


Granulocyte-colony-stimulating factor (G-CSF) stimulates the proliferation and differentiation of cells of the neutrophil lineage by interaction with a specific receptor. Early signal transduction events following G-CSF receptor activation were studied. We detected tyrosine phosphorylation of both the G-CSF receptor and the protein tyrosine kinase JAK1 following G-CSF binding to the human G-CSF receptor. In vitro, the kinase activity of JAK1 was increased by G-CSF stimulation. Coimmunoprecipitation of JAK1 with the G-CSF receptor suggested a physical association which existed prior to G-CSF stimulation.

Pubmed ID: 7512720


  • Nicholson SE
  • Oates AC
  • Harpur AG
  • Ziemiecki A
  • Wilks AF
  • Layton JE


Proceedings of the National Academy of Sciences of the United States of America

Publication Data

April 12, 1994

Associated Grants


Mesh Terms

  • Animals
  • CHO Cells
  • Cell Division
  • Cricetinae
  • Humans
  • Janus Kinase 1
  • Phosphorylation
  • Phosphotyrosine
  • Protein-Tyrosine Kinases
  • Receptors, Granulocyte Colony-Stimulating Factor
  • Signal Transduction
  • Time Factors
  • Transfection
  • Tyrosine