This protein binds tointerleukin-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 bindinterleukin-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 theimmunodeficiency of patients with severemycobacterial andSalmonella infections.[6] Two alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.[5]
All mutations known in theIL12RB1 gene, as well as many polymorphisms, have been collected in a mutation database[7][8]
van de Vosse E, Lichtenauer-Kaligis EG, van Dissel JT, Ottenhoff TH (March 2003). "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.doi:10.1007/s00251-002-0534-9.PMID12671732.S2CID34119140.
Gillessen S, Carvajal D, Ling P, Podlaski FJ, Stremlo DL, Familletti PC, et al. (January 1995). "Mouse interleukin-12 (IL-12) p40 homodimer: a potent IL-12 antagonist".European Journal of Immunology.25 (1):200–206.doi:10.1002/eji.1830250133.PMID7843232.S2CID41702014.
Chua AO, Chizzonite R, Desai BB, Truitt TP, Nunes P, Minetti LJ, et al. (July 1994). "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.doi:10.4049/jimmunol.153.1.128.PMID7911493.S2CID9211163.
Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides".Gene.138 (1–2):171–174.doi:10.1016/0378-1119(94)90802-8.PMID8125298.
Yamamoto K, Kobayashi H, Miura O, Hirosawa S, Miyasaka N (1997). "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.doi:10.1159/000134589.PMID9284929.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library".Gene.200 (1–2):149–156.doi:10.1016/S0378-1119(97)00411-3.PMID9373149.
de Jong R, Altare F, Haagen IA, Elferink DG, Boer T, van Breda Vriesman PJ, et al. (May 1998). "Severe mycobacterial and Salmonella infections in interleukin-12 receptor-deficient patients".Science.280 (5368):1435–1438.Bibcode:1998Sci...280.1435D.doi:10.1126/science.280.5368.1435.PMID9603733.
Kawashima T, Kawasaki H, Kitamura T, Nojima Y, Morimoto C (May 1998). "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.doi:10.1006/cimm.1998.1294.PMID9637763.
Yao BB, Niu P, Surowy CS, Faltynek CR (August 1999). "Direct interaction of STAT4 with the IL-12 receptor".Archives of Biochemistry and Biophysics.368 (1):147–155.doi:10.1006/abbi.1999.1302.PMID10415122.
