TI  - Expression cloning of a receptor for human granulocyte-macrophage
      colony-stimulating factor.
PG  - 3667-76
AB  - Two cDNA clones encoding a receptor for human <prot>granulocyte-macrophage
      colony-stimulating factor</prot> (<prot>hGM-CSF-R</prot>) were isolated by expression
      screening of a library made from human placental mRNA. Pools of
      recombinant plasmid DNA were electroporated into COS cells which were then
      screened for their capacity to bind radioiodinated hGM-CSF using a
      sensitive microscopic autoradiographic approach. The cloned <prot>GM-CSF-R</prot>
      precursor is a 400 amino acid polypeptide (Mr 45,000) with a single
      transmembrane domain, a glycosylated extracellular domain and a short (54
      amino acids) intracytoplasmic tail. It does not contain a tyrosine kinase
      domain nor show homology with members of the immunoglobulin super gene
      family, but does show some significant sequence homologies with receptors
      for several other haemopoietic growth factors, including those for
      <prot>interleukin-6</prot>, <prot>erythropoietin</prot> and <prot>interleukin-2</prot> (beta-chain) and also to
      the prolactin receptor. When transfected into COS cells the cloned cDNA
      directed the expression of a  <prot>GM-CSF-R</prot>  showing a single class of affinity
      (KD = 2(-8) nM) and specificity for human  <prot>GM-CSF</prot>  but not <prot>interleukin-3</prot>.
      Messenger RNA coding for this receptor was detected in a variety of
      haemopoietic cells known to display <prot>hGM-CSF</prot> binding, and cross-linking
      experiments revealed a similar size for the glycosylated receptors in
      transfected COS and haemopoietic cells.
AD  - Walter and Eliza Hall Institute of Medical Research, Royal Melbourne
