Functional domains of the granulocyte colony-stimulating factor receptor.

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Abstract
The granulocyte colony‐stimulating factor (G‐CSF) receptor has a composite structure consisting of an immunoglobulin(Ig)‐like domain, a cytokine receptor‐homologous (CRH) domain and three fibronectin type III (FNIII) domains in the extracellular region. Introduction of G‐CSF receptor cDNA into IL‐3‐dependent murine myeloid cell line FDC‐P1 and pro‐B cell line BAF‐B03, which normally do not respond to G‐CSF, enabled them to proliferate in response to G‐CSF. On the other hand, expression of the G‐CSF receptor cDNA in the IL‐2‐dependent T cell line CTLL‐2 did not enable it to grow in response to G‐CSF, although G‐CSF could transiently stimulate DNA synthesis. Mutational analyses of the G‐CSF receptor in FDC‐P1 cells indicated that the N‐terminal half of the CRH domain was essential for the recognition of G‐CSF, but the Ig‐like, FNIII and cytoplasmic domains were not. The CRH domain and a portion of the cytoplasmic domain of about 100 amino acids in length were indispensable for transduction of the G‐CSF‐triggered growth signal.