
The diverse biological activities of G-CSF are initiated by the binding of G-CSF to a specific receptor (G-CSFR) that belongs to the cytokine/hematopoietic receptor superfamily. In contrast to the majority of hematopoietic receptors that are activated through the formation of heteromeric complexes composed of α, β and sometimes γ subunits, G-CSFR proteins are believed to form homodimeric complexes upon ligand binding. Four distinct alternative splice variants of G-CSFR have been described, one of which exists as a soluble receptor protein. Although G-CSFR lacks consensus motifs in its cytoplasmic domains that are characteristic of kinase activities, certain sequences have been identified that are conserved among several members of the cytokine receptor superfamily. For example, the carboxy terminal regions of G-CSFR contain a domain, designated box 3, that is only shared with the IL-6R subunit, gp130.
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