ArticleThe EMBO journal1991
Identification of the second subunit of the murine interleukin-5 receptor: interleukin-3 receptor-like protein, AIC2B is a component of the high affinity interleukin-5 receptor.
Article in The EMBO journal, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 145 citations in OpenAlex.
- Transcriptional Regulation of the Human IL5RA Gene through Alternative Promoter Usage during Eosinophil Development.International journal of molecular sciences · 2021Article
- Structural basis of interleukin-5 dimer recognition by its α receptor.Protein science : a publication of the Protein Society · 2012Article
- Interleukin-5 and IL-5 receptor in health and diseases.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2011Review
- Spred-1 negatively regulates allergen-induced airway eosinophilia and hyperresponsiveness.The Journal of experimental medicine · 2005Article
- Article
- A critical role of Lyn and Fyn for B cell responses to CD38 ligation and interleukin 5.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Preferential proliferation of murine colony-forming units in culture in a chemically defined condition with a macrophage colony-stimulating factor-negative stromal cell clone.The Journal of experimental medicine · 1996Article
- The murine DUB-1 gene is specifically induced by the betac subunit of interleukin-3 receptor.Molecular and cellular biology · 1996Article
- IL-6 cytokine family and signal transduction: a model of the cytokine system.Journal of molecular medicine (Berlin, Germany) · 1996Review
- CD38 ligation induces tyrosine phosphorylation of Bruton tyrosine kinase and enhanced expression of interleukin 5-receptor alpha chain: synergistic effects with interleukin 5.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Detailed analysis of the IL-5-IL-5R alpha interaction: characterization of crucial residues on the ligand and the receptor.The EMBO journal · 1995Article
- Raf-1 protein is required for growth factor-induced proliferation of hematopoietic cells.The Journal of experimental medicine · 1995Article
- Identification of receptor-binding domains on human interleukin 5 and design of an interleukin 5-derived receptor antagonist.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Impaired interleukin-3 (IL-3) response of the A/J mouse is caused by a branch point deletion in the IL-3 receptor alpha subunit gene.The EMBO journal · 1995Article
- Multi-colony stimulating activity of interleukin 5 (IL-5) on hematopoietic progenitors from transgenic mice that express IL-5 receptor alpha subunit constitutively.The Journal of experimental medicine · 1995Article
- IL-5 receptor-mediated tyrosine phosphorylation of SH2/SH3-containing proteins and activation of Bruton's tyrosine and Janus 2 kinases.The Journal of experimental medicine · 1994Article
- A critical cytoplasmic domain of the interleukin-5 (IL-5) receptor alpha chain and its function in IL-5-mediated growth signal transduction.Molecular and cellular biology · 1994Article
- Activation and inhibition of erythropoietin receptor function: role of receptor dimerization.Molecular and cellular biology · 1994Article
- Hematopoietic cell phosphatase associates with the interleukin-3 (IL-3) receptor beta chain and down-regulates IL-3-induced tyrosine phosphorylation and mitogenesis.Molecular and cellular biology · 1993Article
- Signal transduction by the high-affinity GM-CSF receptor: two distinct cytoplasmic regions of the common beta subunit responsible for different signaling.The EMBO journal · 1993Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Murine interleukin-5 (IL-5) binds to its receptor with high and low affinity. It has been shown that the high affinity IL-5 receptor (IL-5-R) is composed of at least two membrane protein subunits and is responsible for IL-5-mediated signal transduction. One subunit of the high affinity IL-5-R is a 60 kDa membrane protein (p60 IL-5-R) whose cDNA was isolated using the anti-IL-5-R monoclonal antibody (mAb), H7. This subunit alone binds IL-5 with low affinity. The second subunit does not bind IL-5 by itself, and is expressed not only on IL-5-dependent cell lines but also on an IL-3-dependent cell line, FDC-P1. Expression of the p60 IL-5-R cDNA in FDC-P1 cells, which do not bind IL-5, reconstituted the high affinity IL-5-R. We have characterized the second subunit of the IL-5-R by using another anti-IL-5-R mAb, R52.120, and the anti-IL-3-R mAb, anti-Aic-2. The anti-Aic-2 mAb down-regulated binding of IL-5 to an IL-5-dependent cell line, Y16. Both R52.120 and anti-Aic-2 mAbs recognized membrane proteins of 130-140 kDa expressed on FDC-P1 and Y16 cells. The R52.120 mAb recognized both murine IL-3-R (AIC2A) and its homologue (AIC2B) expressed on L cells transfected with suitable cDNAs. The high affinity IL-5-R was reconstituted on an L cell transfectant co-expressing AIC2B and p60 IL-5-R, whereas only the low affinity IL-5-R was detected on a transfectant co-expressing AIC2A and p60 IL-5-R.(ABSTRACT TRUNCATED AT 250 WORDS)
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