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{{About|the CISH gene||Cytokine-inducible SH2-containing protein||CIS (disambiguation){{!}}CIS}}
{{PBB_Controls
{{Infobox_gene}}
| update_page = yes
'''Cytokine-inducible SH2-containing protein''' is a [[protein]] that in humans is encoded by the ''CISH'' [[gene]].<ref name="pmid9465889">{{cite journal | vauthors = Uchida K, Yoshimura A, Inazawa J, Yanagisawa K, Osada H, Masuda A, Saito T, Takahashi T, Miyajima A, Takahashi T | title = Molecular cloning of CISH, chromosome assignment to 3p21.3, and analysis of expression in fetal and adult tissues | journal = Cytogenetics and Cell Genetics | volume = 78 | issue = 3-4 | pages = 209–12 | date = Mar 1998 | pmid = 9465889 | pmc =  | doi = 10.1159/000134658 }}</ref><ref name="pmid7796808">{{cite journal | vauthors = Yoshimura A, Ohkubo T, Kiguchi T, Jenkins NA, Gilbert DJ, Copeland NG, Hara T, Miyajima A | title = A novel cytokine-inducible gene CIS encodes an SH2-containing protein that binds to tyrosine-phosphorylated interleukin 3 and erythropoietin receptors | journal = The EMBO Journal | volume = 14 | issue = 12 | pages = 2816–26 | date = Jun 1995 | pmid = 7796808 | pmc = 398400 | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CISH cytokine inducible SH2-containing protein| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1154| accessdate = }}</ref> ''CISH'' [[orthologs]] <ref name="OrthoMaM">{{cite web | title = OrthoMaM phylogenetic marker: CISH coding sequence | url = http://www.orthomam.univ-montp2.fr/orthomam/data/cds/detailMarkers/ENSG00000114737_CISH.xml }}</ref> have been identified in most [[mammals]] with sequenced genomes. CISH controls T cell receptor (TCR) signaling, and variations of ''CISH'' with certain SNPs are associated with susceptibility to bacteremia, tuberculosis and malaria.<ref name="Khor">{{cite journal | vauthors = Khor CC, Vannberg FO, Chapman SJ, Guo H, Wong SH, Walley AJ, Vukcevic D, Rautanen A, Mills TC, Chang KC, Kam KM, Crampin AC, Ngwira B, Leung CC, Tam CM, Chan CY, Sung JJ, Yew WW, Toh KY, Tay SK, Kwiatkowski D, Lienhardt C, Hien TT, Day NP, Peshu N, Marsh K, Maitland K, Scott JA, Williams TN, Berkley JA, Floyd S, Tang NL, Fine PE, Goh DL, Hill AV | title = CISH and susceptibility to infectious diseases | journal = The New England Journal of Medicine | volume = 362 | issue = 22 | pages = 2092–101 | date = Jun 2010 | pmid = 20484391 | doi = 10.1056/NEJMoa0905606 | url = http://content.nejm.org/cgi/pmidlookup?view=short&pmid=20484391&promo=ONFLNS19 }} [Free Text]</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Cytokine inducible SH2-containing protein
| HGNCid = 1984
| Symbol = CISH
| AltSymbols =; CIS; CIS-1; G18; SOCS
| OMIM = 602441
| ECnumber = 
| Homologene = 7667
| MGIid = 103159
| GeneAtlas_image1 = PBB_GE_CISH_221223_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}}
| Process = {{GNF_GO|id=GO:0001558 |text = regulation of cell growth}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0009968 |text = negative regulation of signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1154
    | Hs_Ensembl = ENSG00000114737
    | Hs_RefseqProtein = NP_659508
    | Hs_RefseqmRNA = NM_145071
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 50618925
    | Hs_GenLoc_end = 50624207
    | Hs_Uniprot = Q9NSE2
    | Mm_EntrezGene = 12700
    | Mm_Ensembl = ENSMUSG00000032578
    | Mm_RefseqmRNA = NM_009895
    | Mm_RefseqProtein = NP_034025
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 107143623
    | Mm_GenLoc_end = 107160885
    | Mm_Uniprot = Q8C3F4
  }}
}}
'''Cytokine inducible SH2-containing protein''', also known as '''CISH''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CISH cytokine inducible SH2-containing protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1154| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein encoded by this gene contains a [[SH2 domain]] and a [[Suppressor of cytokine signalling|SOCS box domain]]. The protein thus belongs to the [[cytokine-induced STAT inhibitor]] (CIS), also known as suppressor of cytokine signaling (SOCS) or STAT-induced STAT inhibitor (SSI), protein family. [[CIS protein family|CIS family]] members are known to be cytokine-inducible negative regulators of cytokine signaling.
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene contains a SH2 domain and a SOCS box domain. The protein thus belongs to the cytokine-induced STAT inhibitor (CIS), also known as suppressor of cytokine signaling (SOCS) or STAT-induced STAT inhibitor (SSI), protein family. CIS family members are known to be cytokine-inducible negative regulators of cytokine signaling. The expression of this gene can be induced by IL2, IL3, GM-CSF and EPO in hematopoietic cells. Proteasome-mediated degradation of this protein has been shown to be involved in the inactivation of the erythropoietin receptor.<ref name="entrez">{{cite web | title = Entrez Gene: CISH cytokine inducible SH2-containing protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1154| accessdate = }}</ref>
}}


==References==
The expression of this gene can be induced by IL-2, IL-3, GM-CSF and EPO in [[hematopoietic]] cells. [[Proteasome]]-mediated degradation of this protein has been shown to be involved in the inactivation of the [[erythropoietin receptor]].<ref name="entrez" />
{{reflist|2}}
 
==Further reading==
CISH is induced by [[T cell receptor]] (TCR) ligation and negatively regulates it by targeting the critical signaling intermediate [[PLCG1|PLC-gamma-1]] for degradation.<ref name = "Palmer_2015">{{cite journal | vauthors = Palmer DC, Guittard GC, Franco Z, Crompton JG, Eil RL, Patel SJ, Ji Y, Van Panhuys N, Klebanoff CA, Sukumar M, Clever D, Chichura A, Roychoudhuri R, Varma R, Wang E, Gattinoni L, Marincola FM, Balagopalan L, Samelson LE, Restifo NP | title = Cish actively silences TCR signaling in CD8+ T cells to maintain tumor tolerance | journal = The Journal of Experimental Medicine | date = Nov 2015 | pmid = 26527801 | doi = 10.1084/jem.20150304 | pmc=4647263 | volume=212 | pages=2095–113}}</ref> The deletion of Cish in effector T cells has been shown to augment TCR signaling and subsequent effector cytokine release, proliferation and survival. The adoptive transfer of tumor-specific effector T cells knocked out or knocked down for CISH resulted in a significant increase in functional avidity and long-term tumor immunity. There are no changes in activity or phosphorylation of Cish's purported target, [[STAT5]] in either the presence or absence of Cish.
{{refbegin | 2}}
 
{{PBB_Further_reading
==Model organisms==
| citations =  
{| class="wikitable sortable collapsible collapsed" border="1" cellpadding="2" style="float: right;" |
*{{cite journal | author=Kile BT, Schulman BA, Alexander WS, ''et al.'' |title=The SOCS box: a tale of destruction and degradation. |journal=Trends Biochem. Sci. |volume=27 |issue= 5 |pages= 235-41 |year= 2002 |pmid= 12076535 |doi= }}
|+ ''Cish'' knockout mouse phenotype
*{{cite journal  | author=Yoshimura A, Ohkubo T, Kiguchi T, ''et al.'' |title=A novel cytokine-inducible gene CIS encodes an SH2-containing protein that binds to tyrosine-phosphorylated interleukin 3 and erythropoietin receptors. |journal=EMBO J. |volume=14 |issue= 12 |pages= 2816-26 |year= 1995 |pmid= 7796808 |doi=  }}
|-
*{{cite journal  | author=Uchida K, Yoshimura A, Inazawa J, ''et al.'' |title=Molecular cloning of CISH, chromosome assignment to 3p21.3, and analysis of expression in fetal and adult tissues. |journal=Cytogenet. Cell Genet. |volume=78 |issue= 3-4 |pages= 209-12 |year= 1998 |pmid= 9465889 |doi=  }}
! Characteristic!! Phenotype
*{{cite journal  | author=Verdier F, Chrétien S, Muller O, ''et al.'' |title=Proteasomes regulate erythropoietin receptor and signal transducer and activator of transcription 5 (STAT5) activation. Possible involvement of the ubiquitinated Cis protein. |journal=J. Biol. Chem. |volume=273 |issue= 43 |pages= 28185-90 |year= 1998 |pmid= 9774439 |doi=  }}
 
*{{cite journal  | author=Aman MJ, Migone TS, Sasaki A, ''et al.'' |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 |year= 1999 |pmid= 10514520 |doi=  }}
|-
*{{cite journal  | author=Okabe S, Tauchi T, Morita H, ''et al.'' |title=Thrombopoietin induces an SH2-containing protein, CIS1, which binds to Mpl: involvement of the ubiquitin proteosome pathway. |journal=Exp. Hematol. |volume=27 |issue= 10 |pages= 1542-7 |year= 1999 |pmid= 10517496 |doi=  }}
| [[Homozygote]] viability || bgcolor="#488ED3"|Normal
*{{cite journal  | author=Jiang C, Yu L, Zhao Y, ''et al.'' |title=Cloning and characterization of CIS 1b (cytokine inducible SH2-containing protein 1b), an alternative splicing form of CIS 1 gene. |journal=DNA Seq. |volume=11 |issue= 1-2 |pages= 149-54 |year= 2000 |pmid= 10902923 |doi=  }}
|-
*{{cite journal  | author=Dogusan Z, Hooghe-Peters EL, Berus D, ''et al.'' |title=Expression of SOCS genes in normal and leukemic human leukocytes stimulated by prolactin, growth hormone and cytokines. |journal=J. Neuroimmunol. |volume=109 |issue= 1 |pages= 34-9 |year= 2000 |pmid= 10969179 |doi= }}
| Fertility || bgcolor="#488ED3"|Normal
*{{cite journal  | author=Yousefi S, Cooper PR, Mueck B, ''et al.'' |title=cDNA representational difference analysis of human neutrophils stimulated by GM-CSF. |journal=Biochem. Biophys. Res. Commun. |volume=277 |issue= 2 |pages= 401-9 |year= 2000 |pmid= 11032736 |doi= 10.1006/bbrc.2000.3678 }}
|-
*{{cite journal  | author=Dif F, Saunier E, Demeneix B, ''et al.'' |title=Cytokine-inducible SH2-containing protein suppresses PRL signaling by binding the PRL receptor. |journal=Endocrinology |volume=142 |issue= 12 |pages= 5286-93 |year= 2001 |pmid= 11713228 |doi=  }}
| Body weight || bgcolor="#488ED3"|Normal
*{{cite journal  | author=Federici M, Giustizieri ML, Scarponi C, ''et al.'' |title=Impaired IFN-gamma-dependent inflammatory responses in human keratinocytes overexpressing the suppressor of cytokine signaling 1. |journal=J. Immunol. |volume=169 |issue= 1 |pages= 434-42 |year= 2002 |pmid= 12077274 |doi=  }}
|-
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
| [[Open Field (animal test)|Anxiety]] || bgcolor="#488ED3"|Normal
*{{cite journal | author=Du L, Frick GP, Tai LR, ''et al.'' |title=Interaction of the growth hormone receptor with cytokine-induced Src homology domain 2 protein in rat adipocytes. |journal=Endocrinology |volume=144 |issue= 3 |pages= 868-76 |year= 2003 |pmid= 12586763 |doi=  }}
|-
*{{cite journal | author=Chen S, Anderson PO, Li L, ''et al.'' |title=Functional association of cytokine-induced SH2 protein and protein kinase C in activated T cells. |journal=Int. Immunol. |volume=15 |issue= 3 |pages= 403-9 |year= 2003 |pmid= 12618484 |doi= }}
| Neurological assessment || bgcolor="#488ED3"|Normal
*{{cite journal | author=Yamasaki K, Hanakawa Y, Tokumaru S, ''et al.'' |title=Suppressor of cytokine signaling 1/JAB and suppressor of cytokine signaling 3/cytokine-inducible SH2 containing protein 3 negatively regulate the signal transducers and activators of transcription signaling pathway in normal human epidermal keratinocytes. |journal=J. Invest. Dermatol. |volume=120 |issue= 4 |pages= 571-80 |year= 2003 |pmid= 12648219 |doi= 10.1046/j.1523-1747.2003.12100.x }}
|-
*{{cite journal | author=Cheng J, Zhang D, Zhou C, Marasco WA |title=Down-regulation of SHP1 and up-regulation of negative regulators of JAK/STAT signaling in HTLV-1 transformed cell lines and freshly transformed human peripheral blood CD4+ T-cells. |journal=Leuk. Res. |volume=28 |issue= 1 |pages= 71-82 |year= 2004 |pmid= 14630083 |doi= }}
| Grip strength || bgcolor="#488ED3"|Normal
*{{cite journal | author=Bayle J, Letard S, Frank R, ''et al.'' |title=Suppressor of cytokine signaling 6 associates with KIT and regulates KIT receptor signaling. |journal=J. Biol. Chem. |volume=279 |issue= 13 |pages= 12249-59 |year= 2004 |pmid= 14707129 |doi= 10.1074/jbc.M313381200 }}
|-
*{{cite journal | author=Colland F, Jacq X, Trouplin V, ''et al.'' |title=Functional proteomics mapping of a human signaling pathway. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324-32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104 }}
| [[Hot plate test|Hot plate]] || bgcolor="#488ED3"|Normal
*{{cite journal | author=Hunter MG, Jacob A, O'donnell LC, ''et al.'' |title=Loss of SHIP and CIS recruitment to the granulocyte colony-stimulating factor receptor contribute to hyperproliferative responses in severe congenital neutropenia/acute myelogenous leukemia. |journal=J. Immunol. |volume=173 |issue= 8 |pages= 5036-45 |year= 2004 |pmid= 15470047 |doi=  }}
|-
}}
| [[Dysmorphology]] || bgcolor="#488ED3"|Normal
|-
| [[Indirect calorimetry]] || bgcolor="#488ED3"|Normal
|-
| [[Glucose tolerance test]] || bgcolor="#488ED3"|Normal
|-
| [[Auditory brainstem response]] || bgcolor="#488ED3"|Normal
|-
| [[Dual-energy X-ray absorptiometry|DEXA]] || bgcolor="#488ED3"|Normal
|-
| [[Radiography]] || bgcolor="#488ED3"|Normal
|-
| Body temperature || bgcolor="#488ED3"|Normal
|-
| Eye morphology || bgcolor="#488ED3"|Normal
|-
| [[Clinical chemistry]] || bgcolor="#488ED3"|Normal
|-
| [[Haematology]] || bgcolor="#488ED3"|Normal
|-
| [[Peripheral blood lymphocyte]]s || bgcolor="#488ED3"|Normal
|-
| [[Micronucleus test]] || bgcolor="#488ED3"|Normal
|-
| Heart weight || bgcolor="#488ED3"|Normal
|-
| Skin Histopathology || bgcolor="#488ED3"|Normal
|-
| Eye Histopathology || bgcolor="#488ED3"|Normal
|-
| ''[[Salmonella]]'' infection || bgcolor="#488ED3"|Normal<ref name="''Salmonella'' infection">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MATB/salmonella-challenge/ |title=''Salmonella'' infection data for Cish |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| ''[[Citrobacter]]'' infection || bgcolor="#488ED3"|Normal<ref name="''Citrobacter'' infection">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MATB/citrobacter-challenge/ |title=''Citrobacter'' infection data for Cish |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| colspan=2; style="text-align: center;" | All tests and analysis from<ref name="mgp_reference">{{cite journal| doi = 10.1111/j.1755-3768.2010.4142.x| title = The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice| year = 2010| author = Gerdin AK| journal = Acta Ophthalmologica| volume = 88| issue = S248 }}</ref><ref>[http://www.sanger.ac.uk/mouseportal/ Mouse Resources Portal], Wellcome Trust Sanger Institute.</ref>
|}
[[Model organism]]s have been used in the study of CISH function. A conditional [[knockout mouse]] line, called ''Cish<sup>tm1a(KOMP)Wtsi</sup>''<ref name="allele_ref">{{cite web |url=http://www.knockoutmouse.org/martsearch/search?query=Cish |title=International Knockout Mouse Consortium}}</ref><ref name="mgi_allele_ref">{{cite web |url=http://www.informatics.jax.org/searchtool/Search.do?query=MGI:4362236 |title=Mouse Genome Informatics}}</ref> was generated as part of the [[International Knockout Mouse Consortium]] program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the [[Wellcome Trust Sanger Institute]].<ref name="pmid21677750">{{cite journal | vauthors = Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A | title = A conditional knockout resource for the genome-wide study of mouse gene function | journal = Nature | volume = 474 | issue = 7351 | pages = 337–42 | date = Jun 2011 | pmid = 21677750 | pmc = 3572410 | doi = 10.1038/nature10163 }}</ref><ref name="mouse_library">{{cite journal | vauthors = Dolgin E | title = Mouse library set to be knockout | journal = Nature | volume = 474 | issue = 7351 | pages = 262–3 | date = Jun 2011 | pmid = 21677718 | doi = 10.1038/474262a }}</ref><ref name="mouse_for_all_reasons">{{cite journal | vauthors = Collins FS, Rossant J, Wurst W | title = A mouse for all reasons | journal = Cell | volume = 128 | issue = 1 | pages = 9–13 | date = Jan 2007 | pmid = 17218247 | doi = 10.1016/j.cell.2006.12.018 }}</ref>
 
Male and female animals underwent a standardized [[phenotypic screen]] to determine the effects of deletion.<ref name="mgp_reference" /><ref name="pmid21722353">{{cite journal | vauthors = van der Weyden L, White JK, Adams DJ, Logan DW | title = The mouse genetics toolkit: revealing function and mechanism | journal = Genome Biology | volume = 12 | issue = 6 | pages = 224 | year = 2011 | pmid = 21722353 | pmc = 3218837 | doi = 10.1186/gb-2011-12-6-224 }}</ref> Twenty four tests were carried out on [[mutant]] mice, however no significant abnormalities were observed.<ref name="mgp_reference" />
 
== Interactions ==
 
CISH has been shown to [[Protein-protein interaction|interact]] with [[IL2RB]]<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 = The Journal of Biological Chemistry | volume = 274 | issue = 42 | pages = 30266–72 | date = Oct 1999 | pmid = 10514520 | doi = 10.1074/jbc.274.42.30266 }}</ref> and [[Growth hormone receptor]].<ref name=pmid10585430>{{cite journal | vauthors = Ram PA, Waxman DJ | title = SOCS/CIS protein inhibition of growth hormone-stimulated STAT5 signaling by multiple mechanisms | journal = The Journal of Biological Chemistry | volume = 274 | issue = 50 | pages = 35553–61 | date = Dec 1999 | pmid = 10585430 | doi = 10.1074/jbc.274.50.35553 }}</ref> and [[PLCG1]].<ref name = "Palmer_2015"/>
 
== References ==
{{reflist|33em}}
 
== Further reading ==
{{refbegin|33em}}
* {{cite journal | vauthors = Kile BT, Schulman BA, Alexander WS, Nicola NA, Martin HM, Hilton DJ | title = The SOCS box: a tale of destruction and degradation | journal = Trends in Biochemical Sciences | volume = 27 | issue = 5 | pages = 235–41 | date = May 2002 | pmid = 12076535 | doi = 10.1016/S0968-0004(02)02085-6 }}
* {{cite journal | vauthors = Verdier F, Chrétien S, Muller O, Varlet P, Yoshimura A, Gisselbrecht S, Lacombe C, Mayeux P | title = Proteasomes regulate erythropoietin receptor and signal transducer and activator of transcription 5 (STAT5) activation. Possible involvement of the ubiquitinated Cis protein | journal = The Journal of Biological Chemistry | volume = 273 | issue = 43 | pages = 28185–90 | date = Oct 1998 | pmid = 9774439 | doi = 10.1074/jbc.273.43.28185 }}
* {{cite journal | vauthors = Okabe S, Tauchi T, Morita H, Ohashi H, Yoshimura A, Ohyashiki K | title = Thrombopoietin induces an SH2-containing protein, CIS1, which binds to Mpl: involvement of the ubiquitin proteosome pathway | journal = Experimental Hematology | volume = 27 | issue = 10 | pages = 1542–7 | date = Oct 1999 | pmid = 10517496 | doi = 10.1016/S0301-472X(99)00094-6 }}
* {{cite journal | vauthors = Jiang C, Yu L, Zhao Y, Zhang M, Liu Q, Mao N, Geng Z, Zhao S | title = Cloning and characterization of CIS 1b (cytokine inducible SH2-containing protein 1b), an alternative splicing form of CIS 1 gene | journal = DNA Sequence | volume = 11 | issue = 1-2 | pages = 149–54 | year = 2000 | pmid = 10902923 | doi = 10.3109/10425170009033983 }}
* {{cite journal | vauthors = Dogusan Z, Hooghe-Peters EL, Berus D, Velkeniers B, Hooghe R | title = Expression of SOCS genes in normal and leukemic human leukocytes stimulated by prolactin, growth hormone and cytokines | journal = Journal of Neuroimmunology | volume = 109 | issue = 1 | pages = 34–9 | date = Sep 2000 | pmid = 10969179 | doi = 10.1016/S0165-5728(00)00300-3 }}
* {{cite journal | vauthors = Yousefi S, Cooper PR, Mueck B, Potter SL, Jarai G | title = cDNA representational difference analysis of human neutrophils stimulated by GM-CSF | journal = Biochemical and Biophysical Research Communications | volume = 277 | issue = 2 | pages = 401–9 | date = Oct 2000 | pmid = 11032736 | doi = 10.1006/bbrc.2000.3678 }}
* {{cite journal | vauthors = Dif F, Saunier E, Demeneix B, Kelly PA, Edery M | title = Cytokine-inducible SH2-containing protein suppresses PRL signaling by binding the PRL receptor | journal = Endocrinology | volume = 142 | issue = 12 | pages = 5286–93 | date = Dec 2001 | pmid = 11713228 | doi = 10.1210/endo.142.12.8549 }}
* {{cite journal | vauthors = Federici M, Giustizieri ML, Scarponi C, Girolomoni G, Albanesi C | title = Impaired IFN-gamma-dependent inflammatory responses in human keratinocytes overexpressing the suppressor of cytokine signaling 1 | journal = Journal of Immunology | volume = 169 | issue = 1 | pages = 434–42 | date = Jul 2002 | pmid = 12077274 | doi = 10.4049/jimmunol.169.1.434 }}
* {{cite journal | vauthors = Du L, Frick GP, Tai LR, Yoshimura A, Goodman HM | title = Interaction of the growth hormone receptor with cytokine-induced Src homology domain 2 protein in rat adipocytes | journal = Endocrinology | volume = 144 | issue = 3 | pages = 868–76 | date = Mar 2003 | pmid = 12586763 | doi = 10.1210/en.2002-220830 }}
* {{cite journal | vauthors = Chen S, Anderson PO, Li L, Sjögren HO, Wang P, Li SL | title = Functional association of cytokine-induced SH2 protein and protein kinase C in activated T cells | journal = [[International Immunology]] | volume = 15 | issue = 3 | pages = 403–9 | date = Mar 2003 | pmid = 12618484 | doi = 10.1093/intimm/dxg039 }}
* {{cite journal | vauthors = Yamasaki K, Hanakawa Y, Tokumaru S, Shirakata Y, Sayama K, Hanada T, Yoshimura A, Hashimoto K | title = Suppressor of cytokine signaling 1/JAB and suppressor of cytokine signaling 3/cytokine-inducible SH2 containing protein 3 negatively regulate the signal transducers and activators of transcription signaling pathway in normal human epidermal keratinocytes | journal = The Journal of Investigative Dermatology | volume = 120 | issue = 4 | pages = 571–80 | date = Apr 2003 | pmid = 12648219 | doi = 10.1046/j.1523-1747.2003.12100.x }}
* {{cite journal | vauthors = Cheng J, Zhang D, Zhou C, Marasco WA | title = Down-regulation of SHP1 and up-regulation of negative regulators of JAK/STAT signaling in HTLV-1 transformed cell lines and freshly transformed human peripheral blood CD4+ T-cells | journal = Leukemia Research | volume = 28 | issue = 1 | pages = 71–82 | date = Jan 2004 | pmid = 14630083 | doi = 10.1016/S0145-2126(03)00158-9 }}
* {{cite journal | vauthors = Bayle J, Letard S, Frank R, Dubreuil P, De Sepulveda P | title = Suppressor of cytokine signaling 6 associates with KIT and regulates KIT receptor signaling | journal = The Journal of Biological Chemistry | volume = 279 | issue = 13 | pages = 12249–59 | date = Mar 2004 | pmid = 14707129 | doi = 10.1074/jbc.M313381200 }}
* {{cite journal | vauthors = Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM | title = Functional proteomics mapping of a human signaling pathway | journal = Genome Research | volume = 14 | issue = 7 | pages = 1324–32 | date = Jul 2004 | pmid = 15231748 | pmc = 442148 | doi = 10.1101/gr.2334104 }}
* {{cite journal | vauthors = Hunter MG, Jacob A, O'donnell LC, Agler A, Druhan LJ, Coggeshall KM, Avalos BR | title = Loss of SHIP and CIS recruitment to the granulocyte colony-stimulating factor receptor contribute to hyperproliferative responses in severe congenital neutropenia/acute myelogenous leukemia | journal = Journal of Immunology | volume = 173 | issue = 8 | pages = 5036–45 | date = Oct 2004 | pmid = 15470047 | doi = 10.4049/jimmunol.173.8.5036 }}
{{refend}}
{{refend}}


{{protein-stub}}
==External links==
{{WikiDoc Sources}}
* {{UCSC gene info|CISH}}
 
[[Category:Genes mutated in mice]]

Latest revision as of 05:20, 15 June 2018

This article is about the CISH gene. For other uses, see Cytokine-inducible SH2-containing protein.
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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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Cytokine-inducible SH2-containing protein is a protein that in humans is encoded by the CISH gene.[1][2][3] CISH orthologs [4] have been identified in most mammals with sequenced genomes. CISH controls T cell receptor (TCR) signaling, and variations of CISH with certain SNPs are associated with susceptibility to bacteremia, tuberculosis and malaria.[5]

Function

The protein encoded by this gene contains a SH2 domain and a SOCS box domain. The protein thus belongs to the cytokine-induced STAT inhibitor (CIS), also known as suppressor of cytokine signaling (SOCS) or STAT-induced STAT inhibitor (SSI), protein family. CIS family members are known to be cytokine-inducible negative regulators of cytokine signaling.

The expression of this gene can be induced by IL-2, IL-3, GM-CSF and EPO in hematopoietic cells. Proteasome-mediated degradation of this protein has been shown to be involved in the inactivation of the erythropoietin receptor.[3]

CISH is induced by T cell receptor (TCR) ligation and negatively regulates it by targeting the critical signaling intermediate PLC-gamma-1 for degradation.[6] The deletion of Cish in effector T cells has been shown to augment TCR signaling and subsequent effector cytokine release, proliferation and survival. The adoptive transfer of tumor-specific effector T cells knocked out or knocked down for CISH resulted in a significant increase in functional avidity and long-term tumor immunity. There are no changes in activity or phosphorylation of Cish's purported target, STAT5 in either the presence or absence of Cish.

Model organisms

Model organisms have been used in the study of CISH function. A conditional knockout mouse line, called Cishtm1a(KOMP)Wtsi[11][12] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the Wellcome Trust Sanger Institute.[13][14][15]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[9][16] Twenty four tests were carried out on mutant mice, however no significant abnormalities were observed.[9]

Interactions

CISH has been shown to interact with IL2RB[17] and Growth hormone receptor.[18] and PLCG1.[6]

References

  1. ↑ Uchida K, Yoshimura A, Inazawa J, Yanagisawa K, Osada H, Masuda A, Saito T, Takahashi T, Miyajima A, Takahashi T (Mar 1998). "Molecular cloning of CISH, chromosome assignment to 3p21.3, and analysis of expression in fetal and adult tissues". Cytogenetics and Cell Genetics. 78 (3–4): 209–12. doi:10.1159/000134658. PMID 9465889.
  2. ↑ Yoshimura A, Ohkubo T, Kiguchi T, Jenkins NA, Gilbert DJ, Copeland NG, Hara T, Miyajima A (Jun 1995). "A novel cytokine-inducible gene CIS encodes an SH2-containing protein that binds to tyrosine-phosphorylated interleukin 3 and erythropoietin receptors". The EMBO Journal. 14 (12): 2816–26. PMC 398400. PMID 7796808.
  3. ↑ 3.0 3.1 "Entrez Gene: CISH cytokine inducible SH2-containing protein".
  4. ↑ "OrthoMaM phylogenetic marker: CISH coding sequence".
  5. ↑ Khor CC, Vannberg FO, Chapman SJ, Guo H, Wong SH, Walley AJ, Vukcevic D, Rautanen A, Mills TC, Chang KC, Kam KM, Crampin AC, Ngwira B, Leung CC, Tam CM, Chan CY, Sung JJ, Yew WW, Toh KY, Tay SK, Kwiatkowski D, Lienhardt C, Hien TT, Day NP, Peshu N, Marsh K, Maitland K, Scott JA, Williams TN, Berkley JA, Floyd S, Tang NL, Fine PE, Goh DL, Hill AV (Jun 2010). "CISH and susceptibility to infectious diseases". The New England Journal of Medicine. 362 (22): 2092–101. doi:10.1056/NEJMoa0905606. PMID 20484391. [Free Text]
  6. ↑ 6.0 6.1 Palmer DC, Guittard GC, Franco Z, Crompton JG, Eil RL, Patel SJ, Ji Y, Van Panhuys N, Klebanoff CA, Sukumar M, Clever D, Chichura A, Roychoudhuri R, Varma R, Wang E, Gattinoni L, Marincola FM, Balagopalan L, Samelson LE, Restifo NP (Nov 2015). "Cish actively silences TCR signaling in CD8+ T cells to maintain tumor tolerance". The Journal of Experimental Medicine. 212: 2095–113. doi:10.1084/jem.20150304. PMC 4647263. PMID 26527801.
  7. ↑ "Salmonella infection data for Cish". Wellcome Trust Sanger Institute.
  8. ↑ "Citrobacter infection data for Cish". Wellcome Trust Sanger Institute.
  9. ↑ 9.0 9.1 9.2 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88 (S248). doi:10.1111/j.1755-3768.2010.4142.x.
  10. ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  11. ↑ "International Knockout Mouse Consortium".
  12. ↑ "Mouse Genome Informatics".
  13. ↑ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  14. ↑ Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  15. ↑ Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  16. ↑ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biology. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
  17. ↑ Aman MJ, Migone TS, Sasaki A, Ascherman DP, Zhu MH, Soldaini E, Imada K, Miyajima A, Yoshimura A, Leonard WJ (Oct 1999). "CIS associates with the interleukin-2 receptor beta chain and inhibits interleukin-2-dependent signaling". The Journal of Biological Chemistry. 274 (42): 30266–72. doi:10.1074/jbc.274.42.30266. PMID 10514520.
  18. ↑ Ram PA, Waxman DJ (Dec 1999). "SOCS/CIS protein inhibition of growth hormone-stimulated STAT5 signaling by multiple mechanisms". The Journal of Biological Chemistry. 274 (50): 35553–61. doi:10.1074/jbc.274.50.35553. PMID 10585430.

Further reading

  • Kile BT, Schulman BA, Alexander WS, Nicola NA, Martin HM, Hilton DJ (May 2002). "The SOCS box: a tale of destruction and degradation". Trends in Biochemical Sciences. 27 (5): 235–41. doi:10.1016/S0968-0004(02)02085-6. PMID 12076535.
  • Verdier F, Chrétien S, Muller O, Varlet P, Yoshimura A, Gisselbrecht S, Lacombe C, Mayeux P (Oct 1998). "Proteasomes regulate erythropoietin receptor and signal transducer and activator of transcription 5 (STAT5) activation. Possible involvement of the ubiquitinated Cis protein". The Journal of Biological Chemistry. 273 (43): 28185–90. doi:10.1074/jbc.273.43.28185. PMID 9774439.
  • Okabe S, Tauchi T, Morita H, Ohashi H, Yoshimura A, Ohyashiki K (Oct 1999). "Thrombopoietin induces an SH2-containing protein, CIS1, which binds to Mpl: involvement of the ubiquitin proteosome pathway". Experimental Hematology. 27 (10): 1542–7. doi:10.1016/S0301-472X(99)00094-6. PMID 10517496.
  • Jiang C, Yu L, Zhao Y, Zhang M, Liu Q, Mao N, Geng Z, Zhao S (2000). "Cloning and characterization of CIS 1b (cytokine inducible SH2-containing protein 1b), an alternative splicing form of CIS 1 gene". DNA Sequence. 11 (1–2): 149–54. doi:10.3109/10425170009033983. PMID 10902923.
  • Dogusan Z, Hooghe-Peters EL, Berus D, Velkeniers B, Hooghe R (Sep 2000). "Expression of SOCS genes in normal and leukemic human leukocytes stimulated by prolactin, growth hormone and cytokines". Journal of Neuroimmunology. 109 (1): 34–9. doi:10.1016/S0165-5728(00)00300-3. PMID 10969179.
  • Yousefi S, Cooper PR, Mueck B, Potter SL, Jarai G (Oct 2000). "cDNA representational difference analysis of human neutrophils stimulated by GM-CSF". Biochemical and Biophysical Research Communications. 277 (2): 401–9. doi:10.1006/bbrc.2000.3678. PMID 11032736.
  • Dif F, Saunier E, Demeneix B, Kelly PA, Edery M (Dec 2001). "Cytokine-inducible SH2-containing protein suppresses PRL signaling by binding the PRL receptor". Endocrinology. 142 (12): 5286–93. doi:10.1210/endo.142.12.8549. PMID 11713228.
  • Federici M, Giustizieri ML, Scarponi C, Girolomoni G, Albanesi C (Jul 2002). "Impaired IFN-gamma-dependent inflammatory responses in human keratinocytes overexpressing the suppressor of cytokine signaling 1". Journal of Immunology. 169 (1): 434–42. doi:10.4049/jimmunol.169.1.434. PMID 12077274.
  • Du L, Frick GP, Tai LR, Yoshimura A, Goodman HM (Mar 2003). "Interaction of the growth hormone receptor with cytokine-induced Src homology domain 2 protein in rat adipocytes". Endocrinology. 144 (3): 868–76. doi:10.1210/en.2002-220830. PMID 12586763.
  • Chen S, Anderson PO, Li L, Sjögren HO, Wang P, Li SL (Mar 2003). "Functional association of cytokine-induced SH2 protein and protein kinase C in activated T cells". International Immunology. 15 (3): 403–9. doi:10.1093/intimm/dxg039. PMID 12618484.
  • Yamasaki K, Hanakawa Y, Tokumaru S, Shirakata Y, Sayama K, Hanada T, Yoshimura A, Hashimoto K (Apr 2003). "Suppressor of cytokine signaling 1/JAB and suppressor of cytokine signaling 3/cytokine-inducible SH2 containing protein 3 negatively regulate the signal transducers and activators of transcription signaling pathway in normal human epidermal keratinocytes". The Journal of Investigative Dermatology. 120 (4): 571–80. doi:10.1046/j.1523-1747.2003.12100.x. PMID 12648219.
  • Cheng J, Zhang D, Zhou C, Marasco WA (Jan 2004). "Down-regulation of SHP1 and up-regulation of negative regulators of JAK/STAT signaling in HTLV-1 transformed cell lines and freshly transformed human peripheral blood CD4+ T-cells". Leukemia Research. 28 (1): 71–82. doi:10.1016/S0145-2126(03)00158-9. PMID 14630083.
  • Bayle J, Letard S, Frank R, Dubreuil P, De Sepulveda P (Mar 2004). "Suppressor of cytokine signaling 6 associates with KIT and regulates KIT receptor signaling". The Journal of Biological Chemistry. 279 (13): 12249–59. doi:10.1074/jbc.M313381200. PMID 14707129.
  • Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (Jul 2004). "Functional proteomics mapping of a human signaling pathway". Genome Research. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
  • Hunter MG, Jacob A, O'donnell LC, Agler A, Druhan LJ, Coggeshall KM, Avalos BR (Oct 2004). "Loss of SHIP and CIS recruitment to the granulocyte colony-stimulating factor receptor contribute to hyperproliferative responses in severe congenital neutropenia/acute myelogenous leukemia". Journal of Immunology. 173 (8): 5036–45. doi:10.4049/jimmunol.173.8.5036. PMID 15470047.

External links

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