Mc Clure, B.Woodcock, J.Harrison-Findik, D.Lopez, A.D'Andrea, R.2006-06-262006-06-262001Cytokine, 2001; 13(4):240-2431043-46661096-0023http://hdl.handle.net/2440/9391The stoichiometry of the granulocyte-macrophage colony-stimulating factor (GM-CSF) receptor complex is still unresolved. We have utilised a sensitive, functional assay for receptor homodimerisation to show that GM-CSF induces dimerisation of the common signalling subunit, hbeta(c). We generated a chimeric cytokine receptor in which the extracellular and transmembrane domains of hbeta(c)are fused to the cytoplasmic domain of erythropoietin receptor (EPO-R). Given that to induce EPO-R activation and mitogenic signalling there is a requirement for formation of a specific homodimeric complex, we reasoned that the cytoplasmic domain of EPO-R could be utilised as a highly sensitive reporter for functional homodimer formation. We show that, in the presence of a cytoplasmically truncated GM-CSF alpha-subunit, the hbetac-EPO receptor chimera transduces a mitogenic signal in BaF-B03 in response to GM-CSF. This is consistent with formation of a hbeta(c)homodimer following GM-CSF binding and implies that ligand stimulation induces formation of a higher order complex that contains the hbeta(c)homodimer.enCell LineAnimalsHumansMiceGranulocyte-Macrophage Colony-Stimulating FactorReceptors, Cell SurfaceReceptors, Granulocyte-Macrophage Colony-Stimulating FactorRecombinant Fusion ProteinsSignal TransductionProtein BindingDimerizationCytokine Receptor Common beta SubunitJournal article002001101410.1006/cyto.2000.08260001674215000072-s2.0-003592504361642Lopez, A. [0000-0001-7430-0135]