Biology:IL2RB

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


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Interleukin-2 receptor subunit beta is a protein that in humans is encoded by the IL2RB gene.[1] Also known as CD122; IL15RB; P70-75.[1]

Function

The interleukin 2 receptor, which is involved in T cell-mediated immune responses, is present in 3 forms with respect to ability to bind interleukin 2. The low affinity form is a monomer of the alpha subunit (also called CD25) and is not involved in signal transduction. The intermediate affinity form consists of a gamma/beta subunit heterodimer, while the high affinity form consists of an alpha/beta/gamma subunit heterotrimer. Both the intermediate and high affinity forms of the receptor are involved in receptor-mediated endocytosis and transduction of mitogenic signals from interleukin 2. The protein encoded by this gene represents the beta subunit and is a type I membrane protein.[1]

This protein also forms one of the three subunits of the IL-15 receptor.

Activation of the receptor increases proliferation of CD8+ effector T cells.[2]

Interactions

IL2RB has been shown to interact with:

See also

References

  1. 1.0 1.1 1.2 "Entrez Gene: IL2RB interleukin 2 receptor, beta". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3560. 
  2. "The role of interleukin-2 during homeostasis and activation of the immune system". Nat Rev Immunol 12 (3): 180–190. February 17, 2012. doi:10.1038/nri3156. PMID 22343569. 
  3. "CIS associates with the interleukin-2 receptor beta chain and inhibits interleukin-2-dependent signaling". J. Biol. Chem. 274 (42): 30266–72. October 1999. doi:10.1074/jbc.274.42.30266. PMID 10514520. 
  4. "Ubiquitin-independent binding of Hrs mediates endosomal sorting of the interleukin-2 receptor beta-chain". J. Cell Sci. 121 (Pt 10): 1727–38. May 2008. doi:10.1242/jcs.024455. PMID 18445679. 
  5. "Functional activation of Jak1 and Jak3 by selective association with IL-2 receptor subunits". Science 266 (5187): 1045–7. November 1994. doi:10.1126/science.7973659. PMID 7973659. Bibcode1994Sci...266.1045M. 
  6. "Interaction of IL-2R beta and gamma c chains with Jak1 and Jak3: implications for XSCID and XCID". Science 266 (5187): 1042–5. November 1994. doi:10.1126/science.7973658. PMID 7973658. Bibcode1994Sci...266.1042R. https://zenodo.org/record/1231239. 
  7. "Two distinct domains within the N-terminal region of Janus kinase 1 interact with cytokine receptors". J. Immunol. 169 (3): 1302–8. August 2002. doi:10.4049/jimmunol.169.3.1302. PMID 12133952. 
  8. "Delineation of the regions of interleukin-2 (IL-2) receptor beta chain important for association of Jak1 and Jak3. Jak1-independent functional recruitment of Jak3 to Il-2Rbeta". J. Biol. Chem. 273 (17): 10719–25. April 1998. doi:10.1074/jbc.273.17.10719. PMID 9553136. 
  9. "Functional cooperation of the interleukin-2 receptor beta chain and Jak1 in phosphatidylinositol 3-kinase recruitment and phosphorylation". Mol. Cell. Biol. 18 (11): 6416–22. November 1998. doi:10.1128/mcb.18.11.6416. PMID 9774657. 
  10. "Association of STAT1, STAT3 and STAT5 proteins with the IL-2 receptor involves different subdomains of the IL-2 receptor beta chain". Eur. J. Immunol. 30 (1): 59–68. January 2000. doi:10.1002/1521-4141(200001)30:1<59::AID-IMMU59>3.0.CO;2-1. PMID 10602027. 
  11. "The adapter protein Shc interacts with the interleukin-2 (IL-2) receptor upon IL-2 stimulation". J. Biol. Chem. 269 (3): 1599–602. January 1994. doi:10.1016/S0021-9258(17)42066-7. PMID 8294403. 

Further reading

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