IL2RB: Difference between revisions

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(→‎Function: It is known to increase proliferation of CD8+ effector T cells.<ref)
 
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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Interleukin-2 receptor subunit beta''' is a [[protein]] that in humans is encoded by the ''IL2RB'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IL2RB interleukin 2 receptor, beta| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3560| accessdate = }}</ref> Also known as '''CD122'''; '''IL15RB'''; '''P70-75'''.<ref name="entrez"/>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_IL2RB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2b5i.
| PDB = {{PDB2|2b5i}}, {{PDB2|2erj}}
| Name = Interleukin 2 receptor, beta
| HGNCid = 6009
| Symbol = IL2RB
| AltSymbols =; CD122; P70-75
| OMIM = 146710
| ECnumber = 
| Homologene = 47955
| MGIid = 96550
| GeneAtlas_image1 = PBB_GE_IL2RB_205291_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004896 |text = hematopoietin/interferon-class (D200-domain) cytokine receptor activity}} {{GNF_GO|id=GO:0004911 |text = interleukin-2 receptor activity}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0009897 |text = external side of plasma membrane}}
| Process = {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0019221 |text = cytokine and chemokine mediated signaling pathway}} {{GNF_GO|id=GO:0045885 |text = positive regulation of survival gene product activity}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3560
    | Hs_Ensembl = ENSG00000100385
    | Hs_RefseqProtein = NP_000869
    | Hs_RefseqmRNA = NM_000878
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 22
    | Hs_GenLoc_start = 35851824
    | Hs_GenLoc_end = 35875908
    | Hs_Uniprot = P14784
    | Mm_EntrezGene = 16185
    | Mm_Ensembl = ENSMUSG00000068227
    | Mm_RefseqmRNA = NM_008368
    | Mm_RefseqProtein = NP_032394
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 15
    | Mm_GenLoc_start = 78307808
    | Mm_GenLoc_end = 78322321
    | Mm_Uniprot = Q3TEQ2
  }}
}}
'''Interleukin 2 receptor, beta''', also known as '''IL2RB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IL2RB interleukin 2 receptor, beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3560| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = 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 and is not involved in signal transduction. The intermediate affinity form consists of an alpha/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.<ref name="entrez">{{cite web | title = Entrez Gene: IL2RB interleukin 2 receptor, beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3560| accessdate = }}</ref>
}}


==See also==
This protein also forms one of the three subunits of the [[IL-15 receptor]].
 
Activation of the receptor increases proliferation of CD8+ effector [[T cell]]s.<ref>{{cite journal
|vauthors=Boyman O, Sprent J |title=The role of interleukin-2 during homeostasis and activation of the immune system
|journal=Nat Rev Immunol  |volume=12  |issue=3  |pages=180–190
|date=February 17, 2012  |doi= 10.1038/nri3156  |pmid=22343569
}}</ref>
 
== Interactions ==
 
IL2RB has been shown to [[Protein-protein interaction|interact]] with:
* [[CISH]],<ref name = pmid10514520>{{cite journal | vauthors = Aman MJ, Migone TS, Sasaki A, Ascherman DP, ((Zhu Mh)), Soldaini E, Imada K, Miyajima A, Yoshimura A, Leonard WJ | title = CIS associates with the interleukin-2 receptor beta chain and inhibits interleukin-2-dependent signaling | journal = J. Biol. Chem. | volume = 274 | issue = 42 | pages = 30266–72  | date = October 1999 | pmid = 10514520 | doi =  10.1074/jbc.274.42.30266}}</ref>
* [[HGS (gene)|HGS]],<ref name = pmid18445679>{{cite journal | vauthors = Yamashita Y, Kojima K, Tsukahara T, Agawa H, Yamada K, Amano Y, Kurotori N, Tanaka N, Sugamura K, Takeshita T | title = Ubiquitin-independent binding of Hrs mediates endosomal sorting of the interleukin-2 receptor beta-chain | journal = J. Cell Sci. | volume = 121 | issue = Pt 10 | pages = 1727–38  | date = May 2008 | pmid = 18445679 | doi = 10.1242/jcs.024455 }}</ref>
* [[Janus kinase 1]],<ref name = pmid7973659>{{cite journal | vauthors = Miyazaki T, Kawahara A, Fujii H, Nakagawa Y, Minami Y, Liu ZJ, Oishi I, Silvennoinen O, Witthuhn BA, Ihle JN | title = Functional activation of Jak1 and Jak3 by selective association with IL-2 receptor subunits | journal = Science | volume = 266 | issue = 5187 | pages = 1045–7  | date = November 1994 | pmid = 7973659 | doi =  10.1126/science.7973659}}</ref><ref name = pmid7973658>{{cite journal | vauthors = Russell SM, Johnston JA, Noguchi M, Kawamura M, Bacon CM, Friedmann M, Berg M, McVicar DW, Witthuhn BA, Silvennoinen O | title = Interaction of IL-2R beta and gamma c chains with Jak1 and Jak3: implications for XSCID and XCID | journal = Science | volume = 266 | issue = 5187 | pages = 1042–5  | date = November 1994 | pmid = 7973658 | doi =  10.1126/science.7973658}}</ref><ref name = pmid12133952>{{cite journal | vauthors = Usacheva A, Kotenko S, Witte MM, Colamonici OR | title = Two distinct domains within the N-terminal region of Janus kinase 1 interact with cytokine receptors | journal = J. Immunol. | volume = 169 | issue = 3 | pages = 1302–8  | date = August 2002 | pmid = 12133952 | doi =  10.4049/jimmunol.169.3.1302}}</ref><ref name = pmid9553136>{{cite journal | vauthors = Zhu MH, Berry JA, Russell SM, Leonard WJ | title = 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 | journal = J. Biol. Chem. | volume = 273 | issue = 17 | pages = 10719–25  | date = April 1998 | pmid = 9553136 | doi =  10.1074/jbc.273.17.10719}}</ref><ref name = pmid9774657>{{cite journal | vauthors = Migone TS, Rodig S, Cacalano NA, Berg M, Schreiber RD, Leonard WJ | title = Functional cooperation of the interleukin-2 receptor beta chain and Jak1 in phosphatidylinositol 3-kinase recruitment and phosphorylation | journal = Mol. Cell. Biol. | volume = 18 | issue = 11 | pages = 6416–22  | date = November 1998 | pmid = 9774657 | pmc = 109227 | doi =  10.1128/mcb.18.11.6416}}</ref>  and
* [[SHC1]].<ref name = pmid10602027>{{cite journal | vauthors = Delespine-Carmagnat M, Bouvier G, Bertoglio J | title = Association of STAT1, STAT3 and STAT5 proteins with the IL-2 receptor involves different subdomains of the IL-2 receptor beta chain | journal = Eur. J. Immunol. | volume = 30 | issue = 1 | pages = 59–68  | date = January 2000 | pmid = 10602027 | doi = 10.1002/1521-4141(200001)30:1<59::AID-IMMU59>3.0.CO;2-1 }}</ref><ref name = pmid8294403>{{cite journal | vauthors = Ravichandran KS, Burakoff SJ | title = The adapter protein Shc interacts with the interleukin-2 (IL-2) receptor upon IL-2 stimulation | journal = J. Biol. Chem. | volume = 269 | issue = 3 | pages = 1599–602  | date = January 1994 | pmid = 8294403 | doi =  }}</ref>
 
== See also ==
* [[IL-2 receptor]]
* [[IL-2 receptor]]
* [[IL-15 receptor]]


==References==
== References ==
{{reflist|2}}
{{reflist}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Ellery JM, Nicholls PJ | title = Alternate signalling pathways from the interleukin-2 receptor | journal = Cytokine Growth Factor Rev. | volume = 13 | issue = 1 | pages = 27–40 | year = 2002 | pmid = 11750878 | doi = 10.1016/S1359-6101(01)00023-5 }}
| citations =
* {{cite journal | vauthors = Purvis SF, Georges DL, Williams TM, Lederman MM | title = Suppression of interleukin-2 and interleukin-2 receptor expression in Jurkat cells stably expressing the human immunodeficiency virus Tat protein | journal = Cell. Immunol. | volume = 144 | issue = 1 | pages = 32–42 | year = 1992 | pmid = 1394441 | doi = 10.1016/0008-8749(92)90223-C }}
*{{cite journal | author=Ellery JM, Nicholls PJ |title=Alternate signalling pathways from the interleukin-2 receptor. |journal=Cytokine Growth Factor Rev. |volume=13 |issue= 1 |pages= 27-40 |year= 2002 |pmid= 11750878 |doi= }}
* {{cite journal | vauthors = Torigoe T, Saragovi HU, Reed JC | title = Interleukin 2 regulates the activity of the lyn protein-tyrosine kinase in a B-cell line | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 89 | issue = 7 | pages = 2674–8 | year = 1992 | pmid = 1557373 | pmc = 48724 | doi = 10.1073/pnas.89.7.2674 }}
*{{cite journal | author=Purvis SF, Georges DL, Williams TM, Lederman MM |title=Suppression of interleukin-2 and interleukin-2 receptor expression in Jurkat cells stably expressing the human immunodeficiency virus Tat protein. |journal=Cell. Immunol. |volume=144 |issue= 1 |pages= 32-42 |year= 1992 |pmid= 1394441 |doi= }}
* {{cite journal | vauthors = Maslinski W, Remillard B, Tsudo M, Strom TB | title = Interleukin-2 (IL-2) induces tyrosine kinase-dependent translocation of active raf-1 from the IL-2 receptor into the cytosol | journal = J. Biol. Chem. | volume = 267 | issue = 22 | pages = 15281–4 | year = 1992 | pmid = 1639773 | doi =  }}
*{{cite journal | author=Torigoe T, Saragovi HU, Reed JC |title=Interleukin 2 regulates the activity of the lyn protein-tyrosine kinase in a B-cell line. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 7 |pages= 2674-8 |year= 1992 |pmid= 1557373 |doi= }}
* {{cite journal | vauthors = Miyazaki T, Maruyama M, Yamada G, Hatakeyama M, Taniguchi T | title = The integrity of the conserved 'WS motif' common to IL-2 and other cytokine receptors is essential for ligand binding and signal transduction | journal = EMBO J. | volume = 10 | issue = 11 | pages = 3191–7 | year = 1991 | pmid = 1915291 | pmc = 453042 | doi =  }}
*{{cite journal | author=Maslinski W, Remillard B, Tsudo M, Strom TB |title=Interleukin-2 (IL-2) induces tyrosine kinase-dependent translocation of active raf-1 from the IL-2 receptor into the cytosol. |journal=J. Biol. Chem. |volume=267 |issue= 22 |pages= 15281-4 |year= 1992 |pmid= 1639773 |doi=  }}
* {{cite journal | vauthors = Shibuya H, Yoneyama M, Nakamura Y, Harada H, Hatakeyama M, Minamoto S, Kono T, Doi T, White R, Taniguchi T | title = The human interleukin-2 receptor beta-chain gene: genomic organization, promoter analysis and chromosomal assignment | journal = Nucleic Acids Res. | volume = 18 | issue = 13 | pages = 3697–703 | year = 1990 | pmid = 1973832 | pmc = 331067 | doi = 10.1093/nar/18.13.3697 }}
*{{cite journal | author=Miyazaki T, Maruyama M, Yamada G, ''et al.'' |title=The integrity of the conserved 'WS motif' common to IL-2 and other cytokine receptors is essential for ligand binding and signal transduction. |journal=EMBO J. |volume=10 |issue= 11 |pages= 3191-7 |year= 1991 |pmid= 1915291 |doi=  }}
* {{cite journal | vauthors = Hatakeyama M, Kono T, Kobayashi N, Kawahara A, Levin SD, Perlmutter RM, Taniguchi T | title = Interaction of the IL-2 receptor with the src-family kinase p56lck: identification of novel intermolecular association | journal = Science | volume = 252 | issue = 5012 | pages = 1523–8 | year = 1991 | pmid = 2047859 | doi = 10.1126/science.2047859 }}
*{{cite journal | author=Shibuya H, Yoneyama M, Nakamura Y, ''et al.'' |title=The human interleukin-2 receptor beta-chain gene: genomic organization, promoter analysis and chromosomal assignment. |journal=Nucleic Acids Res. |volume=18 |issue= 13 |pages= 3697-703 |year= 1990 |pmid= 1973832 |doi= }}
* {{cite journal | vauthors = Mills GB, May C, McGill M, Fung M, Baker M, Sutherland R, Greene WC | title = Interleukin 2-induced tyrosine phosphorylation. Interleukin 2 receptor beta is tyrosine phosphorylated | journal = J. Biol. Chem. | volume = 265 | issue = 6 | pages = 3561–7 | year = 1990 | pmid = 2303462 | doi =  }}
*{{cite journal | author=Hatakeyama M, Kono T, Kobayashi N, ''et al.'' |title=Interaction of the IL-2 receptor with the src-family kinase p56lck: identification of novel intermolecular association. |journal=Science |volume=252 |issue= 5012 |pages= 1523-8 |year= 1991 |pmid= 2047859 |doi= }}
* {{cite journal | vauthors = Oyaizu N, Chirmule N, Kalyanaraman VS, Hall WW, Pahwa R, Shuster M, Pahwa S | title = Human immunodeficiency virus type 1 envelope glycoprotein gp120 produces immune defects in CD4+ T lymphocytes by inhibiting interleukin 2 mRNA | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 87 | issue = 6 | pages = 2379–83 | year = 1990 | pmid = 2315327 | pmc = 53690 | doi = 10.1073/pnas.87.6.2379 }}
*{{cite journal | author=Mills GB, May C, McGill M, ''et al.'' |title=Interleukin 2-induced tyrosine phosphorylation. Interleukin 2 receptor beta is tyrosine phosphorylated. |journal=J. Biol. Chem. |volume=265 |issue= 6 |pages= 3561-7 |year= 1990 |pmid= 2303462 |doi=  }}
* {{cite journal | vauthors = Gnarra JR, Otani H, Wang MG, McBride OW, Sharon M, Leonard WJ | title = Human interleukin 2 receptor beta-chain gene: chromosomal localization and identification of 5' regulatory sequences | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 87 | issue = 9 | pages = 3440–4 | year = 1990 | pmid = 2333293 | pmc = 53916 | doi = 10.1073/pnas.87.9.3440 }}
*{{cite journal | author=Oyaizu N, Chirmule N, Kalyanaraman VS, ''et al.'' |title=Human immunodeficiency virus type 1 envelope glycoprotein gp120 produces immune defects in CD4+ T lymphocytes by inhibiting interleukin 2 mRNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 6 |pages= 2379-83 |year= 1990 |pmid= 2315327 |doi= }}
* {{cite journal | vauthors = Tsudo M, Kitamura F, Miyasaka M | title = Characterization of the interleukin 2 receptor beta chain using three distinct monoclonal antibodies | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 86 | issue = 6 | pages = 1982–6 | year = 1989 | pmid = 2467293 | pmc = 286829 | doi = 10.1073/pnas.86.6.1982 }}
*{{cite journal | author=Gnarra JR, Otani H, Wang MG, ''et al.'' |title=Human interleukin 2 receptor beta-chain gene: chromosomal localization and identification of 5' regulatory sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 9 |pages= 3440-4 |year= 1990 |pmid= 2333293 |doi= }}
* {{cite journal | vauthors = Hatakeyama M, Tsudo M, Minamoto S, Kono T, Doi T, Miyata T, Miyasaka M, Taniguchi T | title = Interleukin-2 receptor beta chain gene: generation of three receptor forms by cloned human alpha and beta chain cDNA's | journal = Science | volume = 244 | issue = 4904 | pages = 551–6 | year = 1989 | pmid = 2785715 | doi = 10.1126/science.2785715 }}
*{{cite journal | author=Tsudo M, Kitamura F, Miyasaka M |title=Characterization of the interleukin 2 receptor beta chain using three distinct monoclonal antibodies. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 6 |pages= 1982-6 |year= 1989 |pmid= 2467293 |doi= }}
* {{cite journal | vauthors = Kornfeld H, Cruikshank WW, Pyle SW, Berman JS, Center DM | title = Lymphocyte activation by HIV-1 envelope glycoprotein | journal = Nature | volume = 335 | issue = 6189 | pages = 445–8 | year = 1988 | pmid = 2843775 | doi = 10.1038/335445a0 }}
*{{cite journal | author=Hatakeyama M, Tsudo M, Minamoto S, ''et al.'' |title=Interleukin-2 receptor beta chain gene: generation of three receptor forms by cloned human alpha and beta chain cDNA's. |journal=Science |volume=244 |issue= 4904 |pages= 551-6 |year= 1989 |pmid= 2785715 |doi= }}
* {{cite journal | vauthors = Leonard WJ, Donlon TA, Lebo RV, Greene WC | title = Localization of the gene encoding the human interleukin-2 receptor on chromosome 10 | journal = Science | volume = 228 | issue = 4707 | pages = 1547–9 | year = 1985 | pmid = 3925551 | doi = 10.1126/science.3925551 }}
*{{cite journal | author=Kornfeld H, Cruikshank WW, Pyle SW, ''et al.'' |title=Lymphocyte activation by HIV-1 envelope glycoprotein. |journal=Nature |volume=335 |issue= 6189 |pages= 445-8 |year= 1988 |pmid= 2843775 |doi= 10.1038/335445a0 }}
* {{cite journal | vauthors = Bamborough P, Hedgecock CJ, Richards WG | title = The interleukin-2 and interleukin-4 receptors studied by molecular modelling | journal = Structure | volume = 2 | issue = 9 | pages = 839–51 | year = 1994 | pmid = 7529123 | doi = 10.1016/S0969-2126(94)00085-9 }}
*{{cite journal | author=Leonard WJ, Donlon TA, Lebo RV, Greene WC |title=Localization of the gene encoding the human interleukin-2 receptor on chromosome 10. |journal=Science |volume=228 |issue= 4707 |pages= 1547-9 |year= 1985 |pmid= 3925551 |doi= }}
* {{cite journal | vauthors = Minami Y, Nakagawa Y, Kawahara A, Miyazaki T, Sada K, Yamamura H, Taniguchi T | title = Protein tyrosine kinase Syk is associated with and activated by the IL-2 receptor: possible link with the c-myc induction pathway | journal = Immunity | volume = 2 | issue = 1 | pages = 89–100 | year = 1995 | pmid = 7600304 | doi = 10.1016/1074-7613(95)90081-0 }}
*{{cite journal | author=Bamborough P, Hedgecock CJ, Richards WG |title=The interleukin-2 and interleukin-4 receptors studied by molecular modelling. |journal=Structure |volume=2 |issue= 9 |pages= 839-51 |year= 1995 |pmid= 7529123 |doi= }}
* {{cite journal | vauthors = Giri JG, Kumaki S, Ahdieh M, Friend DJ, Loomis A, Shanebeck K, DuBose R, Cosman D, Park LS, Anderson DM | title = Identification and cloning of a novel IL-15 binding protein that is structurally related to the alpha chain of the IL-2 receptor | journal = EMBO J. | volume = 14 | issue = 15 | pages = 3654–63 | year = 1995 | pmid = 7641685 | pmc = 394440 | doi =  }}
*{{cite journal | author=Minami Y, Nakagawa Y, Kawahara A, ''et al.'' |title=Protein tyrosine kinase Syk is associated with and activated by the IL-2 receptor: possible link with the c-myc induction pathway. |journal=Immunity |volume=2 |issue= 1 |pages= 89-100 |year= 1995 |pmid= 7600304 |doi= }}
* {{cite journal | vauthors = Kirken RA, Rui H, Evans GA, Farrar WL | title = Characterization of an interleukin-2 (IL-2)-induced tyrosine phosphorylated 116-kDa protein associated with the IL-2 receptor beta-subunit | journal = J. Biol. Chem. | volume = 268 | issue = 30 | pages = 22765–70 | year = 1993 | pmid = 7693677 | doi =  }}
*{{cite journal | author=Giri JG, Kumaki S, Ahdieh M, ''et al.'' |title=Identification and cloning of a novel IL-15 binding protein that is structurally related to the alpha chain of the IL-2 receptor. |journal=EMBO J. |volume=14 |issue= 15 |pages= 3654-63 |year= 1995 |pmid= 7641685 |doi=  }}
* {{cite journal | vauthors = Puri RK, Leland P, Aggarwal BB | title = Constitutive expression of human immunodeficiency virus type 1 tat gene inhibits interleukin 2 and interleukin 2 receptor expression in a human CD4+ T lymphoid (H9) cell line | journal = AIDS Res. Hum. Retroviruses | volume = 11 | issue = 1 | pages = 31–40 | year = 1995 | pmid = 7734194 | doi = 10.1089/aid.1995.11.31 }}
*{{cite journal | author=Kirken RA, Rui H, Evans GA, Farrar WL |title=Characterization of an interleukin-2 (IL-2)-induced tyrosine phosphorylated 116-kDa protein associated with the IL-2 receptor beta-subunit. |journal=J. Biol. Chem. |volume=268 |issue= 30 |pages= 22765-70 |year= 1993 |pmid= 7693677 |doi=  }}
* {{cite journal | vauthors = Miyazaki T, Liu ZJ, Kawahara A, Minami Y, Yamada K, Tsujimoto Y, Barsoumian EL, Permutter RM, Taniguchi T | title = Three distinct IL-2 signaling pathways mediated by bcl-2, c-myc, and lck cooperate in hematopoietic cell proliferation | journal = Cell | volume = 81 | issue = 2 | pages = 223–31 | year = 1995 | pmid = 7736574 | doi = 10.1016/0092-8674(95)90332-1 }}
*{{cite journal | author=Puri RK, Leland P, Aggarwal BB |title=Constitutive expression of human immunodeficiency virus type 1 tat gene inhibits interleukin 2 and interleukin 2 receptor expression in a human CD4+ T lymphoid (H9) cell line. |journal=AIDS Res. Hum. Retroviruses |volume=11 |issue= 1 |pages= 31-40 |year= 1995 |pmid= 7734194 |doi= }}
*{{cite journal | author=Miyazaki T, Liu ZJ, Kawahara A, ''et al.'' |title=Three distinct IL-2 signaling pathways mediated by bcl-2, c-myc, and lck cooperate in hematopoietic cell proliferation. |journal=Cell |volume=81 |issue= 2 |pages= 223-31 |year= 1995 |pmid= 7736574 |doi= }}
}}
{{refend}}
{{refend}}


{{membrane-protein-stub}}
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{{NLM content}}
{{WikiDoc Sources}}
{{PDB Gallery|geneid=3560}}
{{Cytokine receptors}}
{{Clusters of differentiation}}
{{Interleukin receptor modulators}}

Latest revision as of 02:02, 24 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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".
  2. ↑ Boyman O, Sprent J (February 17, 2012). "The role of interleukin-2 during homeostasis and activation of the immune system". Nat Rev Immunol. 12 (3): 180–190. doi:10.1038/nri3156. PMID 22343569.
  3. ↑ Aman MJ, Migone TS, Sasaki A, Ascherman DP, Zhu Mh, Soldaini E, Imada K, Miyajima A, Yoshimura A, Leonard WJ (October 1999). "CIS associates with the interleukin-2 receptor beta chain and inhibits interleukin-2-dependent signaling". J. Biol. Chem. 274 (42): 30266–72. doi:10.1074/jbc.274.42.30266. PMID 10514520.
  4. ↑ Yamashita Y, Kojima K, Tsukahara T, Agawa H, Yamada K, Amano Y, Kurotori N, Tanaka N, Sugamura K, Takeshita T (May 2008). "Ubiquitin-independent binding of Hrs mediates endosomal sorting of the interleukin-2 receptor beta-chain". J. Cell Sci. 121 (Pt 10): 1727–38. doi:10.1242/jcs.024455. PMID 18445679.
  5. ↑ Miyazaki T, Kawahara A, Fujii H, Nakagawa Y, Minami Y, Liu ZJ, Oishi I, Silvennoinen O, Witthuhn BA, Ihle JN (November 1994). "Functional activation of Jak1 and Jak3 by selective association with IL-2 receptor subunits". Science. 266 (5187): 1045–7. doi:10.1126/science.7973659. PMID 7973659.
  6. ↑ Russell SM, Johnston JA, Noguchi M, Kawamura M, Bacon CM, Friedmann M, Berg M, McVicar DW, Witthuhn BA, Silvennoinen O (November 1994). "Interaction of IL-2R beta and gamma c chains with Jak1 and Jak3: implications for XSCID and XCID". Science. 266 (5187): 1042–5. doi:10.1126/science.7973658. PMID 7973658.
  7. ↑ Usacheva A, Kotenko S, Witte MM, Colamonici OR (August 2002). "Two distinct domains within the N-terminal region of Janus kinase 1 interact with cytokine receptors". J. Immunol. 169 (3): 1302–8. doi:10.4049/jimmunol.169.3.1302. PMID 12133952.
  8. ↑ Zhu MH, Berry JA, Russell SM, Leonard WJ (April 1998). "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. doi:10.1074/jbc.273.17.10719. PMID 9553136.
  9. ↑ Migone TS, Rodig S, Cacalano NA, Berg M, Schreiber RD, Leonard WJ (November 1998). "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. doi:10.1128/mcb.18.11.6416. PMC 109227. PMID 9774657.
  10. ↑ Delespine-Carmagnat M, Bouvier G, Bertoglio J (January 2000). "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. doi:10.1002/1521-4141(200001)30:1<59::AID-IMMU59>3.0.CO;2-1. PMID 10602027.
  11. ↑ Ravichandran KS, Burakoff SJ (January 1994). "The adapter protein Shc interacts with the interleukin-2 (IL-2) receptor upon IL-2 stimulation". J. Biol. Chem. 269 (3): 1599–602. PMID 8294403.

Further reading

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

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