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https://hdl.handle.net/2440/9391
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Type: | Journal article |
Title: | GM-CSF binding to its receptor induces oligomerisation of the common beta-subunit |
Author: | Mc Clure, B. Woodcock, J. Harrison-Findik, D. Lopez, A. D'Andrea, R. |
Citation: | Cytokine, 2001; 13(4):240-243 |
Publisher: | Acadmic Press |
Issue Date: | 2001 |
ISSN: | 1043-4666 1096-0023 |
Abstract: | The 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. |
Keywords: | Cell Line Animals Humans Mice Granulocyte-Macrophage Colony-Stimulating Factor Receptors, Cell Surface Receptors, Granulocyte-Macrophage Colony-Stimulating Factor Recombinant Fusion Proteins Signal Transduction Protein Binding Dimerization Cytokine Receptor Common beta Subunit |
DOI: | 10.1006/cyto.2000.0826 |
Published version: | http://dx.doi.org/10.1006/cyto.2000.0826 |
Appears in Collections: | Aurora harvest 4 Medicine publications |
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