ArticleThe EMBO journal1994
Three residues in the common beta chain of the human GM-CSF, IL-3 and IL-5 receptors are essential for GM-CSF and IL-5 but not IL-3 high affinity binding and interact with Glu21 of GM-CSF.
Article in The EMBO journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 115 citations in OpenAlex.
- PHF6 interacts with the LMO2 complex in T-cell acute lymphoblastic leukemia.Haematologica · 2026Article
- The Cellular and Transcriptomic Early Innate Immune Response to BCG Vaccination in Mice.Cells · 2024Article
- Neutrophil GM-CSF receptor dynamics in acute lung injury.Journal of leukocyte biology · 2019Article
- Article
- A dual role for the N-terminal domain of the IL-3 receptor in cell signalling.Nature communications · 2018Article
- Transcriptome profile of rat genes in injured spinal cord at different stages by RNA-sequencing.BMC genomics · 2017Article
- Intracerebral GM-CSF contributes to transendothelial monocyte migration in APP/PS1 Alzheimer's disease mice.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2016Article
- Article
- The tumor promoting activity of the EP4 receptor for prostaglandin E2 in murine skin.Molecular oncology · 2014Article
- Structural basis of interleukin-5 dimer recognition by its α receptor.Protein science : a publication of the Protein Society · 2012Article
- The role of interchain heterodisulfide formation in activation of the human common beta and mouse betaIL-3 receptors.The Journal of biological chemistry · 2010Article
- Two modes of beta-receptor recognition are mediated by distinct epitopes on mouse and human interleukin-3.The Journal of biological chemistry · 2010Article
- Review
- A cytokine-cytokine interaction in the assembly of higher-order structure and activation of the interleukine-3:receptor complex.PloS one · 2009Article
- Interleukin-5 receptor subunit oligomerization and rearrangement revealed by fluorescence resonance energy transfer imaging.The Journal of biological chemistry · 2008Article
- Slow-dissociation effect of common signaling subunit beta c on IL5 and GM-CSF receptor assembly.Cytokine · 2008Article
- An improved resolution structure of the human beta common receptor involved in IL-3, IL-5 and GM-CSF signalling which gives better definition of the high-affinity binding epitope.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006Article
- Structural and functional hot spots in cytokine receptors.International journal of hematology · 2001Review
- 1H and 15N chemical shift assignments for domain 4 of the common beta-chain of the IL-3, IL-5 and GM-CSF receptors.Journal of biomolecular NMR · 1999Article
- Crucial role of the residue R280 at the F'-G' loop of the human granulocyte/macrophage colony-stimulating factor receptor alpha chain for ligand recognition.The Journal of experimental medicine · 1997Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The beta subunit (beta c) of the receptors for human granulocyte macrophage colony stimulating factor (GM-CSF), interleukin-3 (IL-3) and interleukin-5 (IL-5) is essential for high affinity ligand-binding and signal transduction. An important feature of this subunit is its common nature, being able to interact with GM-CSF, IL-3 and IL-5. Analogous common subunits have also been identified in other receptor systems including gp130 and the IL-2 receptor gamma subunit. It is not clear how common receptor subunits bind multiple ligands. We have used site-directed mutagenesis and binding assays with radiolabelled GM-CSF, IL-3 and IL-5 to identify residues in the beta c subunit involved in affinity conversion for each ligand. Alanine substitutions in the region Tyr365-Ile368 in beta c showed that Tyr365, His367 and Ile368 were required for GM-CSF and IL-5 high affinity binding, whereas Glu366 was unimportant. In contrast, alanine substitutions of these residues only marginally reduced the conversion of IL-3 binding to high affinity by beta c. To identify likely contact points in GM-CSF involved in binding to the 365-368 beta c region we used the GM-CSF mutant eco E21R which is unable to interact with wild-type beta c whilst retaining full GM-CSF receptor alpha chain binding. Eco E21R exhibited greater binding affinity to receptor alpha beta complexes composed of mutant beta chains Y365A, H367A and I368A than to those composed of wild-type beta c or mutant E366A. These results (i) identify the residues Tyr365, His367 and Ile368 as critical for affinity conversion by beta c, (ii) show that high affinity binding of GM-CSF and IL-5 can be dissociated from IL-3 and (iii) suggest that Tyr365, His367 and Ile368 in beta c interact with Glu21 of GM-CSF.
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