Tyrosine kinase JAK1 is associated with the granulocyte-colony-stimulating factor receptor and both become tyrosine-phosphorylated after receptor activation.
SE Nicholson, AC Oates, AG Harpur… - Proceedings of the …, 1994 - National Acad Sciences
SE Nicholson, AC Oates, AG Harpur, A Ziemiecki, AF Wilks, JE Layton
Proceedings of the National Academy of Sciences, 1994•National Acad SciencesGranulocyte-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 …
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 …
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.
National Acad Sciences