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Gene Review

IL5RA  -  interleukin 5 receptor, alpha

Homo sapiens

Synonyms: CD125, CDw125, HSIL5R3, IL-5 receptor subunit alpha, IL-5R subunit alpha, ...
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Disease relevance of IL5RA

  • In summary, our data suggest that increased expression of IL-5R alpha on CD34+ cells favors eosinophilopoiesis and may thus contribute to the subsequent development of blood and tissue eosinophilia, a hallmark of allergic inflammation [1].
  • Radiolabeled recombinant human IL-5 (hIL-5) was used to characterize the IL-5 receptor present on normal human eosinophils and on the myeloid leukemia line HL-60, which can be induced to differentiate into eosinophilic cells [2].
  • 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 [3].
  • The human IL-5-dependent erythroleukemia TF-1 was used as a source of mRNA which was analysed by northern blotting using a cDNA probe for IL-5R alpha [4].
  • Phage display was used to identify sequences that mimic structural determinants in interleukin5 (IL5) for IL5 receptor recognition [5].

High impact information on IL5RA

  • A first class codes for an IL5-specific chain (hIL5R alpha) [6].
  • A second component of the hIL5R is found to be identical to the beta chain of the human granulocyte-macrophage colony-stimulating factor (GM-CSF) high affinity receptor [6].
  • RFX1, -2 and -3 regulate expression of other medically important gene products (for example, interleukin-5 receptor alpha chain, IL-5R alpha) [7].
  • Furthermore, SHPTP2 appeared to physically associate with beta common (betac) chain of the IL-5 receptor (IL-5betacR) [8].
  • IL-5 receptor-mediated tyrosine phosphorylation of SH2/SH3-containing proteins and activation of Bruton's tyrosine and Janus 2 kinases [9].

Biological context of IL5RA

  • Dinucleotide repeat polymorphism in the IL2 and IL5RA genes [10].
  • Localization of the gene encoding the alpha subunit of human interleukin-5 receptor (IL5RA) to chromosome region 3p24-3p26 [11].
  • By direct DNA sequencing in 24 individuals, we identified 22 sequence variants within exons and flanking regions including a 1.5-kb promoter region of IL5RA; 10 common polymorphic sites were selected for genotyping in our asthma cohort (n = 587) [12].
  • IL5RA variant/haplotype information identified in this study will provide valuable information for strategies for the control of asthma [12].
  • In an effort to discover additional polymorphism(s) in genes whose variant(s) have been implicated in asthma, we investigated the genetic polymorphisms in IL5RA to evaluate the gene as a potential candidate for a host genetic study of asthma [12].

Anatomical context of IL5RA


Associations of IL5RA with chemical compounds

  • We found that this property is largely determined by the NH2-terminal module of hIL-5R alpha, and detailed analysis defined D56 and to a lesser extent E58 as important for binding [14].
  • Moreover, endogenous STAT3 was tyrosine phosphorylated and activated in human IL-5-stimulated BaF3 cells ectopically expressing the human IL-5R (BaF3/IL5R) [15].
  • Retinoic acid modulates IL-5 receptor expression and selectively inhibits eosinophil-basophil differentiation of hemopoietic progenitor cells [16].
  • The inhibition of binding IL5 to its receptor by the isothiazolone derivatives is abrogated by free-sulfhydryl-containing compounds such as dithiothreitol, indicating that the isothiazolones react with the sulfhydryl group of free cysteine residues in the hIL5R alpha [17].
  • The results reveal that the arginine residue is crucial for the IL-5Ralpha binding of AF17121, while the acidic residues are not essential though likely complex-stabilizing particularly in the Asp(2)-Glu(3) region [18].

Physical interactions of IL5RA


Regulatory relationships of IL5RA


Other interactions of IL5RA

  • The activation of the JAK2/STAT5 pathway is commonly involved in signaling through the human IL-5 receptor [27].
  • The results suggest that the IL5RA locus is unlinked to other members of the hematopoietic receptor family [11].
  • As a prerequisite to studies of the transcriptional regulation of the IL-5R alpha subunit gene, we used three different methods, including primer extension, RNase protection, and 5'-RACE to precisely map the transcriptional start site to a position 15 base pairs (bp) upstream of the 5' end of the published sequence of IL-5R alpha exon 1 [13].
  • A membrane-proximal proline-rich element of the hIL-5R alpha cytoplasmic domain that is conserved among different members of the hemopoietic cytokine receptor family was essential for biological activity [28].
  • RT-PCR was used to evaluate IL-5 receptor alpha (IL-5R(alpha)) expression in various tissues and to assess bronchus and saphenous vein eosinophils through use of CCR3 expression [29].

Analytical, diagnostic and therapeutic context of IL5RA


  1. Allergen-induced increases in IL-5 receptor alpha-subunit expression on bone marrow-derived CD34+ cells from asthmatic subjects. A novel marker of progenitor cell commitment towards eosinophilic differentiation. Sehmi, R., Wood, L.J., Watson, R., Foley, R., Hamid, Q., O'Byrne, P.M., Denburg, J.A. J. Clin. Invest. (1997) [Pubmed]
  2. Characterization of a receptor for interleukin-5 on human eosinophils and the myeloid leukemia line HL-60. Ingley, E., Young, I.G. Blood (1991) [Pubmed]
  3. 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. Huston, M.M., Moore, J.P., Mettes, H.J., Tavana, G., Huston, D.P. J. Immunol. (1996) [Pubmed]
  4. Interleukin-5 receptor alpha chain mRNA is down-regulated by transforming growth factor beta 1. Zanders, E.D. Eur. Cytokine Netw. (1994) [Pubmed]
  5. Coiled coil miniprotein randomization on phage leads to charge pattern mimicry of the receptor recognition determinant of interleukin 5. Li, C., Plugariu, C.G., Bajgier, J., White, J.R., Liefer, K.M., Wu, S.J., Chaiken, I. J. Mol. Recognit. (2002) [Pubmed]
  6. 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. Tavernier, J., Devos, R., Cornelis, S., Tuypens, T., Van der Heyden, J., Fiers, W., Plaetinck, G. Cell (1991) [Pubmed]
  7. Structure of the winged-helix protein hRFX1 reveals a new mode of DNA binding. Gajiwala, K.S., Chen, H., Cornille, F., Roques, B.P., Reith, W., Mach, B., Burley, S.K. Nature (2000) [Pubmed]
  8. Src homology 2 protein tyrosine phosphatase (SHPTP2)/Src homology 2 phosphatase 2 (SHP2) tyrosine phosphatase is a positive regulator of the interleukin 5 receptor signal transduction pathways leading to the prolongation of eosinophil survival. Pazdrak, K., Adachi, T., Alam, R. J. Exp. Med. (1997) [Pubmed]
  9. IL-5 receptor-mediated tyrosine phosphorylation of SH2/SH3-containing proteins and activation of Bruton's tyrosine and Janus 2 kinases. Sato, S., Katagiri, T., Takaki, S., Kikuchi, Y., Hitoshi, Y., Yonehara, S., Tsukada, S., Kitamura, D., Watanabe, T., Witte, O., Takatsu, K. J. Exp. Med. (1994) [Pubmed]
  10. Dinucleotide repeat polymorphism in the IL2 and IL5RA genes. Epplen, C., Frank, G., Gomolka, M., Nagy, M., Nürnberg, P., Epplen, J.T. Hum. Mol. Genet. (1994) [Pubmed]
  11. Localization of the gene encoding the alpha subunit of human interleukin-5 receptor (IL5RA) to chromosome region 3p24-3p26. Isobe, M., Kumura, Y., Murata, Y., Takaki, S., Tominaga, A., Takatsu, K., Ogita, Z. Genomics (1992) [Pubmed]
  12. Association analysis of interleukin 5 receptor alpha subunit (IL5RA) polymorphisms and asthma. Cheong, H.S., Kim, L.H., Park, B.L., Choi, Y.H., Park, H.S., Hong, S.J., Choi, B.W., Park, C.S., Shin, H.D. J. Hum. Genet. (2005) [Pubmed]
  13. Identification and characterization of a functional promoter region in the human eosinophil IL-5 receptor alpha subunit gene. Sun, Z., Yergeau, D.A., Tuypens, T., Tavernier, J., Paul, C.C., Baumann, M.A., Tenen, D.G., Ackerman, S.J. J. Biol. Chem. (1995) [Pubmed]
  14. Detailed analysis of the IL-5-IL-5R alpha interaction: characterization of crucial residues on the ligand and the receptor. Cornelis, S., Plaetinck, G., Devos, R., Van der Heyden, J., Tavernier, J., Sanderson, C.J., Guisez, Y., Fiers, W. EMBO J. (1995) [Pubmed]
  15. Activation of the STAT3/acute phase response factor transcription factor by interleukin-5. Caldenhoven, E., van Dijk, T., Raaijmakers, J.A., Lammers, J.W., Koenderman, L., De Groot, R.P. J. Biol. Chem. (1995) [Pubmed]
  16. Retinoic acid modulates IL-5 receptor expression and selectively inhibits eosinophil-basophil differentiation of hemopoietic progenitor cells. Upham, J.W., Sehmi, R., Hayes, L.M., Howie, K., Lundahl, J., Denburg, J.A. J. Allergy Clin. Immunol. (2002) [Pubmed]
  17. Covalent modification of the interleukin-5 receptor by isothiazolones leads to inhibition of the binding of interleukin-5. Devos, R., Guisez, Y., Plaetinck, G., Cornelis, S., Tavernier, J., van der Heyden, J., Foley, L.H., Scheffler, J.E. Eur. J. Biochem. (1994) [Pubmed]
  18. Cyclic peptide interleukin 5 antagonists mimic CD turn recognition epitope for receptor alpha. Ruchala, P., Varadi, G., Ishino, T., Scibek, J., Bhattacharya, M., Urbina, C., Ryk, D.V., Uings, I., Chaiken, I. Biopolymers (2004) [Pubmed]
  19. Binding interactions of human interleukin 5 with its receptor alpha subunit. Large scale production, structural, and functional studies of Drosophila-expressed recombinant proteins. Johanson, K., Appelbaum, E., Doyle, M., Hensley, P., Zhao, B., Abdel-Meguid, S.S., Young, P., Cook, R., Carr, S., Matico, R. J. Biol. Chem. (1995) [Pubmed]
  20. Structure of the activation domain of the GM-CSF/IL-3/IL-5 receptor common beta-chain bound to an antagonist. Rossjohn, J., McKinstry, W.J., Woodcock, J.M., McClure, B.J., Hercus, T.R., Parker, M.W., Lopez, A.F., Bagley, C.J. Blood (2000) [Pubmed]
  21. Differential regulation of interleukin 5-stimulated signaling pathways by dynamin. Gorska, M.M., Cen, O., Liang, Q., Stafford, S.J., Alam, R. J. Biol. Chem. (2006) [Pubmed]
  22. Selective inhibition of IL-5 receptor alpha-chain gene transcription by IL-5, IL-3, and granulocyte-macrophage colony-stimulating factor in human blood eosinophils. Wang, P., Wu, P., Cheewatrakoolpong, B., Myers, J.G., Egan, R.W., Billah, M.M. J. Immunol. (1998) [Pubmed]
  23. Interleukin-9 enhances interleukin-5 receptor expression, differentiation, and survival of human eosinophils. Gounni, A.S., Gregory, B., Nutku, E., Aris, F., Latifa, K., Minshall, E., North, J., Tavernier, J., Levit, R., Nicolaides, N., Robinson, D., Hamid, Q. Blood (2000) [Pubmed]
  24. Dimeric RFX proteins contribute to the activity and lineage specificity of the interleukin-5 receptor alpha promoter through activation and repression domains. Iwama, A., Pan, J., Zhang, P., Reith, W., Mach, B., Tenen, D.G., Sun, Z. Mol. Cell. Biol. (1999) [Pubmed]
  25. JAK kinases control IL-5 receptor ubiquitination, degradation, and internalization. Martinez-Moczygemba, M., Huston, D.P., Lei, J.T. J. Leukoc. Biol. (2007) [Pubmed]
  26. Expression of interleukin-5 receptors on acute myeloid leukaemia cells: association with immunophenotype and karyotype. Nishii, K., Kita, K., Nadim, M., Miwa, H., Ohoishi, K., Yamaguchi, M., Shirakawa, S. Br. J. Haematol. (1995) [Pubmed]
  27. The activation of the JAK2/STAT5 pathway is commonly involved in signaling through the human IL-5 receptor. Ogata, N., Kikuchi, Y., Kouro, T., Tomonaga, M., Takatsu, K. Int. Arch. Allergy Immunol. (1997) [Pubmed]
  28. Characterization of critical residues in the cytoplasmic domain of the human interleukin-5 receptor alpha chain required for growth signal transduction. Cornelis, S., Fache, I., Van der Heyden, J., Guisez, Y., Tavernier, J., Devos, R., Fiers, W., Plaetinck, G. Eur. J. Immunol. (1995) [Pubmed]
  29. The IL-5 receptor on human bronchus selectively primes for hyperresponsiveness. Rizzo, C.A., Yang, R., Greenfeder, S., Egan, R.W., Pauwels, R.A., Hey, J.A. J. Allergy Clin. Immunol. (2002) [Pubmed]
  30. Interleukin-5 receptors on human lung eosinophils after segmental allergen challenge. Julius, P., Hochheim, D., Böser, K., Schmidt, S., Myrtek, D., Bachert, C., Luttmann, W., Virchow, J.C. Clin. Exp. Allergy (2004) [Pubmed]
  31. Molecular cloning of the guinea-pig IL-5 receptor alpha and beta subunits and reconstitution of a high affinity receptor. Scott, C.W., Logsdon, N.J., Wilkins, D.E., Norris, T.E., Sobotka-Briner, C., Hubbs, S., Graham, A. Cytokine (2000) [Pubmed]
  32. Monomeric isomers of human interleukin 5 show that 1:1 receptor recruitment is sufficient for function. Li, J., Cook, R., Doyle, M.L., Hensley, P., McNulty, D.E., Chaiken, I. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
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