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. 1994 Apr 12;91(8):2985–2988. doi: 10.1073/pnas.91.8.2985

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

S E Nicholson 1, A C Oates 1, A G Harpur 1, A Ziemiecki 1, A F Wilks 1, J E Layton 1
PMCID: PMC43499  PMID: 7512720

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.

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Selected References

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