Biology:Interleukin 5 receptor alpha subunit

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

Interleukin 5 receptor, alpha (IL5RA) also known as CD125 (Cluster of Differentiation 125) is a subunit of the Interleukin-5 receptor. IL5RA also denotes its human gene.

Function

The protein encoded by this gene is an interleukin 5 specific subunit of a heterodimeric cytokine receptor. The receptor is composed of a ligand specific alpha subunit and a signal transducing beta subunit shared by the receptors for interleukin 3 (IL3), colony stimulating factor 2 (CSF2/GM-CSF), and interleukin 5 (IL5). The binding of this protein to IL5 depends on the beta subunit. The beta subunit is activated by the ligand binding, and is required for the biological activities of IL5. This protein has been found to interact with syndecan binding protein (syntenin), which is required for IL5 mediated activation of the transcription factor SOX4. Six alternatively spliced transcript variants encoding three distinct isoforms have been reported.

Interactions

Interleukin 5 receptor alpha subunit has been shown to interact with:

• Interleukin 5,
• Janus kinase 2,
• Protein unc-119 homolog, and
• SDCBP

See also

• Cluster of differentiation
• Benralizumab
• Mepolizumab
• Reslizumab

Further reading

• "Localization of the gene encoding the alpha subunit of human interleukin-5 receptor (IL5RA) to chromosome region 3p24-3p26.". Genomics 14 (3): 755–8. 1992. doi:10.1016/S0888-7543(05)80180-6. PMID 1427903. 
• "Organization and chromosomal localization of the human interleukin 5 receptor alpha-chain gene.". Eur. Cytokine Netw. 3 (5): 451–9. 1993. PMID 1477296. 
• "Molecular basis of the membrane-anchored and two soluble isoforms of the human interleukin 5 receptor alpha subunit.". Proc. Natl. Acad. Sci. U.S.A. 89 (15): 7041–5. 1992. doi:10.1073/pnas.89.15.7041. PMID 1495999. Bibcode: 1992PNAS...89.7041T. 
• "Structure and sequence of the human alpha-L-iduronidase gene.". Genomics 13 (4): 1311–3. 1992. doi:10.1016/0888-7543(92)90053-U. PMID 1505961. 
• "Molecular cloning and expression of the human interleukin 5 receptor.". J. Exp. Med. 175 (2): 341–51. 1992. doi:10.1084/jem.175.2.341. PMID 1732409. 
• "A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific alpha chain and a beta chain shared with the receptor for GM-CSF.". Cell 66 (6): 1175–84. 1991. doi:10.1016/0092-8674(91)90040-6. PMID 1833065. 
• "Binding interactions of human interleukin 5 with its receptor alpha subunit. Large scale production, structural, and functional studies of Drosophila-expressed recombinant proteins.". J. Biol. Chem. 270 (16): 9459–71. 1995. doi:10.1074/jbc.270.16.9459. PMID 7721873. 
• "Identification and characterization of a functional promoter region in the human eosinophil IL-5 receptor alpha subunit gene.". J. Biol. Chem. 270 (3): 1462–71. 1995. doi:10.1074/jbc.270.3.1462. PMID 7836416. 
• "Regulation of eosinophil migration by adult T cell leukemia-derived factor.". J. Immunol. 151 (10): 5624–30. 1993. doi:10.4049/jimmunol.151.10.5624. PMID 8228251. 
• "Human B cells express IL-5 receptor messenger ribonucleic acid and respond to IL-5 with enhanced IgM production after mitogenic stimulation with Moraxella catarrhalis.". J. Immunol. 156 (4): 1392–401. 1996. doi:10.4049/jimmunol.156.4.1392. PMID 8568239. 
• "Attenuation of IL-5-mediated signal transduction, eosinophil survival, and inflammatory mediator release by a soluble human IL-5 receptor.". J. Immunol. 159 (8): 4024–34. 1997. doi:10.4049/jimmunol.159.8.4024. PMID 9378992. 
• "JAK2 and JAK1 constitutively associate with an interleukin-5 (IL-5) receptor alpha and betac subunit, respectively, and are activated upon IL-5 stimulation.". Blood 91 (7): 2264–71. 1998. doi:10.1182/blood.V91.7.2264. PMID 9516124. 
• "Interleukin 5 regulates the isoform expression of its own receptor alpha-subunit.". Blood 95 (5): 1600–7. 2000. doi:10.1182/blood.V95.5.1600.005k22_1600_1607. PMID 10688814. 
• "Identification of regions within the third FnIII-like domain of the IL-5Ralpha involved in IL-5 interaction.". Cytokine 12 (7): 867–73. 2000. doi:10.1006/cyto.1999.0663. PMID 10880230. 
• "Multisite mutagenesis of interleukin 5 differentiates sites for receptor recognition and receptor activation.". Biochemistry 39 (48): 14939–49. 2001. doi:10.1021/bi001467p. PMID 11101310. 
• "Cytokine-specific transcriptional regulation through an IL-5Ralpha interacting protein.". Science 293 (5532): 1136–8. 2001. doi:10.1126/science.1059157. PMID 11498591. 
• "Retinoic acid modulates IL-5 receptor expression and selectively inhibits eosinophil-basophil differentiation of hemopoietic progenitor cells.". J. Allergy Clin. Immunol. 109 (2): 307–13. 2002. doi:10.1067/mai.2002.121527. PMID 11842302. 
• "The IL-5 receptor on human bronchus selectively primes for hyperresponsiveness.". J. Allergy Clin. Immunol. 109 (3): 404–9. 2002. doi:10.1067/mai.2002.122459. PMID 11897983. 
• "Biosensor analysis of dynamics of interleukin 5 receptor subunit beta(c) interaction with IL5:IL5R(alpha) complexes.". Anal. Biochem. 307 (2): 258–65. 2003. doi:10.1016/S0003-2697(02)00043-X. PMID 12202242. 
• "Decreased expression of membrane IL-5 receptor alpha on human eosinophils: I. Loss of membrane IL-5 receptor alpha on airway eosinophils and increased soluble IL-5 receptor alpha in the airway after allergen challenge.". J. Immunol. 169 (11): 6452–8. 2002. doi:10.4049/jimmunol.169.11.6452. PMID 12444154. 

External links

• IL5RA+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
• Overview of all the structural information available in the PDB for UniProt: Q01344 (Interleukin-5 receptor subunit alpha) at the PDBe-KB.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.