Hematopoietic growth factor receptors

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Abstract
The molecular cloning for most of the hematopoietic growth factor receptors has been achieved over the past few years and revealed that they can by assigned to two discrete receptor families, namely the hematopoietic growth factor superfamily (HRS) and the receptor tyrosine kinase family (RTK). The members of the HRS, including granulocyte‐macrophage colony‐stimulating factor receptor (GM‐CSF‐R), interleukin 3 receptor (IL‐3‐R), granulocyte CSF receptor (G‐CSF‐R) and erythropoietin receptor (Epo‐R), share a common binding domain and the absence of a tyrosine kinase domain in their cytoplasmic portion. In some cases (e.g., GM‐CSF‐R), the high‐affinity receptor structure is obtained through the association of the low‐affinity binding chain (alpha chain) with an accessory protein (beta chain). It is conceivable that this protein might also represent the common subunit shared by GM‐CSF‐R and by IL‐3‐R when they are co‐expressed to form the putative GM‐CSF‐R/IL‐3‐R complex. Although tyrosine phosphorylation following ligand receptor activation seems to be a common event in the HRS, its role in the signal transduction mechanisms is unknown. Due to the structural analogies among the members of this family any new insight into one particular receptor member, such as its subunit structure and its signal transduction pathways, will be gener‐alizable to the other family members.

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