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

Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):2985-8. doi: 10.1073/pnas.91.8.2985.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

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

Substances

  • Receptors, Granulocyte Colony-Stimulating Factor
  • Phosphotyrosine
  • Tyrosine
  • Protein-Tyrosine Kinases
  • JAK1 protein, human
  • Janus Kinase 1