Biology:Interleukin 12 receptor, beta 1 subunit

Short description: Protein and coding gene in humans

Generic protein structure example

Interleukin-12 receptor, beta 1, or IL-12Rβ1 in short, is a subunit of the interleukin 12 receptor and the interleukin 23 receptor. IL12RB1, is the name of its human gene. IL-12Rβ1 is also known as CD212 (cluster of differentiation 212).

The protein encoded by this gene is a type I transmembrane protein that belongs to the hemopoietin receptor superfamily.

This protein binds to interleukin-12 (IL-12) with a low affinity, and is part of the IL-12 receptor complex. This protein forms a disulfide-linked oligomer, which is required for its IL-12 binding activity. The coexpression of this and IL-12Rβ2 protein was shown to lead to the formation of high-affinity IL-12 binding sites and reconstitution of IL-12 dependent signaling.

IL-12Rβ1 can also bind interleukin-23 (IL-23) as part of the IL-23 receptor complex. This complex forms a disulfide-linked oligomer, which is required for its IL-23 binding activity. The coexpression of this and IL-23R protein was shown to lead to the formation of IL-23 binding sites.

Various mutations in this gene were found to result in the immunodeficiency of patients with severe mycobacterial and Salmonella infections. Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.

All mutations known in the IL12RB1 gene, as well as many polymorphisms, have been collected in a mutation database

Further reading

• "Genetic variations in the interleukin-12/interleukin-23 receptor (beta1) chain, and implications for IL-12 and IL-23 receptor structure and function". Immunogenetics 54 (12): 817–829. March 2003. doi:10.1007/s00251-002-0534-9. PMID 12671732. 
• "Human IL-12 p40 homodimer binds to the IL-12 receptor but does not mediate biologic activity". Journal of Immunology 154 (1): 116–127. January 1995. doi:10.4049/jimmunol.154.1.116. PMID 7527811. 
• "Mouse interleukin-12 (IL-12) p40 homodimer: a potent IL-12 antagonist". European Journal of Immunology 25 (1): 200–206. January 1995. doi:10.1002/eji.1830250133. PMID 7843232. 
• "Expression cloning of a human IL-12 receptor component. A new member of the cytokine receptor superfamily with strong homology to gp130". Journal of Immunology 153 (1): 128–136. July 1994. doi:10.4049/jimmunol.153.1.128. PMID 7911493. 
• "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–174. January 1994. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• "A functional interleukin 12 receptor complex is composed of two beta-type cytokine receptor subunits". Proceedings of the National Academy of Sciences of the United States of America 93 (24): 14002–14007. November 1996. doi:10.1073/pnas.93.24.14002. PMID 8943050. Bibcode: 1996PNAS...9314002P. 
• "Molecular biology of interleukin-12 receptors". Annals of the New York Academy of Sciences 795 (1): 36–40. October 1996. doi:10.1111/j.1749-6632.1996.tb52653.x. PMID 8958915. Bibcode: 1996NYASA.795...36G. 
• "Differential associations between the cytoplasmic regions of the interleukin-12 receptor subunits beta1 and beta2 and JAK kinases". The Journal of Biological Chemistry 272 (9): 6073–6077. February 1997. doi:10.1074/jbc.272.9.6073. PMID 9038232. 
• "Assignment of IL12RB1 and IL12RB2, interleukin-12 receptor beta 1 and beta 2 chains, to human chromosome 19 band p13.1 and chromosome 1 band p31.2, respectively, by in situ hybridization". Cytogenetics and Cell Genetics 77 (3–4): 257–258. 1997. doi:10.1159/000134589. PMID 9284929. 
• "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–156. October 1997. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• "IL-12 receptor (IL-12R) expression and accumulation of IL-12R beta 1 and IL-12R beta 2 mRNAs in CD4+ T cells by costimulation with B7-2 molecules". Journal of Immunology 160 (4): 1638–1646. February 1998. doi:10.4049/jimmunol.160.4.1638. PMID 9469420. 
• "Severe mycobacterial and Salmonella infections in interleukin-12 receptor-deficient patients". Science 280 (5368): 1435–1438. May 1998. doi:10.1126/science.280.5368.1435. PMID 9603733. Bibcode: 1998Sci...280.1435D. 
• "Interleukin-12 induces tyrosine phosphorylation of an 85-kDa protein associated with the interleukin-12 receptor beta 1 subunit". Cellular Immunology 186 (1): 39–44. May 1998. doi:10.1006/cimm.1998.1294. PMID 9637763. 
• "Direct interaction of STAT4 with the IL-12 receptor". Archives of Biochemistry and Biophysics 368 (1): 147–155. August 1999. doi:10.1006/abbi.1999.1302. PMID 10415122. 
• "Novel p19 protein engages IL-12p40 to form a cytokine, IL-23, with biological activities similar as well as distinct from IL-12". Immunity 13 (5): 715–725. November 2000. doi:10.1016/S1074-7613(00)00070-4. PMID 11114383. 
• "Interleukin-12 receptor beta1 deficiency in a patient with abdominal tuberculosis". The Journal of Infectious Diseases 184 (2): 231–236. July 2001. doi:10.1086/321999. PMID 11424023. 
• "Requirement for both IL-12 and IFN-gamma signaling pathways in optimal IFN-gamma production by human T cells". European Journal of Immunology 32 (3): 693–700. March 2002. doi:10.1002/1521-4141(200203)32:3<693::AID-IMMU693>3.0.CO;2-Q. PMID 11857344. 
• "A receptor for the heterodimeric cytokine IL-23 is composed of IL-12Rbeta1 and a novel cytokine receptor subunit, IL-23R". Journal of Immunology 168 (11): 5699–5708. June 2002. doi:10.4049/jimmunol.168.11.5699. PMID 12023369. 
• "Impaired accumulation and function of memory CD4 T cells in human IL-12 receptor beta 1 deficiency". Journal of Immunology 170 (1): 597–603. January 2003. doi:10.4049/jimmunol.170.1.597. PMID 12496448. 

External links

• IL12RB1+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

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