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{{Infobox_gene}}
{{Infobox_gene}}
'''Caspase recruitment domain-containing protein 9''' is an [[Signal transducing adaptor protein|adaptor protein]] that in humans is encoded by the ''CARD9'' [[gene]].<ref name="pmid11053425">{{cite journal | vauthors = Bertin J, Guo Y, Wang L, Srinivasula SM, Jacobson MD, Poyet JL, Merriam S, Du MQ, Dyer MJ, Robison KE, DiStefano PS, Alnemri ES | title = CARD9 is a novel caspase recruitment domain-containing protein that interacts with BCL10/CLAP and activates NF-kappa B | journal = J. Biol. Chem. | volume = 275 | issue = 52 | pages = 41082–6 | date = Jan 2001 | pmid = 11053425 | pmc =  | doi = 10.1074/jbc.C000726200 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CARD9 caspase recruitment domain family, member 9| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64170| accessdate = }}</ref>
'''Caspase recruitment domain-containing protein 9''' is an [[Signal transducing adaptor protein|adaptor protein]] which in humans is encoded by the ''CARD9'' [[gene]].<ref name="pmid11053425">{{cite journal | vauthors = Bertin J, Guo Y, Wang L, Srinivasula SM, Jacobson MD, Poyet JL, Merriam S, Du MQ, Dyer MJ, Robison KE, DiStefano PS, Alnemri ES | title = CARD9 is a novel caspase recruitment domain-containing protein that interacts with BCL10/CLAP and activates NF-kappa B | journal = J. Biol. Chem. | volume = 275 | issue = 52 | pages = 41082–6 | date = Jan 2001 | pmid = 11053425 | pmc =  | doi = 10.1074/jbc.C000726200 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CARD9 caspase recruitment domain family, member 9| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64170| accessdate = }}</ref>It mediates signals from pattern recognition receptors to activate pro-inflammatory and anti-inflammatory cytokines,  regulating inflammation and cell [[apoptosis]]. Homozygous mutations in CARD9 are associated with defective innate immunity against yeasts, like Candida and dermatophytes.


== Function ==
== Function ==


CARD9 is a member of the CARD protein family, which is defined by the presence of a characteristic caspase-associated recruitment domain ([[CARD domain|CARD]]). CARD is a protein interaction domain known to participate in activation or suppression of CARD containing members of the [[caspase]] family, and thus plays an important regulatory role in cell [[apoptosis]]. This protein was identified by its selective association with the CARD domain of [[BCL10]], a positive regulator of apoptosis and [[NF-κB]] activation, and is thought to function as a molecular scaffold for the assembly of a BCL10 signaling complex that activates NF-κB. Several alternatively spliced transcript variants have been observed, but their full-length nature is not clearly defined.<ref name="entrez" />
CARD9 is a member of the CARD protein family, which is defined by the presence of a characteristic caspase-associated recruitment domain ([[CARD domain|CARD]]). CARD is a protein interaction domain known to participate in activation or suppression of CARD containing members of the [[caspase]] family, and thus plays an important regulatory role in cell [[apoptosis]]. This protein was identified by its selective association with the CARD domain of [[BCL10]], a positive regulator of apoptosis and [[NF-κB]] activation.<ref name=autogenerated1>{{cite journal | vauthors = Bertin J, Guo Y, Wang L, Srinivasula SM, Jacobson MD, Poyet JL, Merriam S, Du MQ, Dyer MJ, Robison KE, DiStefano PS, Alnemri ES | title = CARD9 is a novel caspase recruitment domain-containing protein that interacts with BCL10/CLAP and activates NF-kappa B | journal = J. Biol. Chem. | volume = 275 | issue = 52 | pages = 41082–6  | date = December 2000 | pmid = 11053425 | doi = 10.1074/jbc.C000726200 }}</ref>It is thought to function as a molecular scaffold for the assembly of a BCL10 signaling complex that activates NF-κB. Several alternatively spliced transcript variants have been observed, but their full-length nature is not clearly defined.<ref name="entrez" />


== Clinical significance ==
== Clinical significance ==


It recently became clear that Card9 plays important roles as part of the innate immune response for the defense against pathogens such as yeasts. Card9 mediates signals from so called pattern recognition receptors ([[CLEC7A|Dectin-1]]) to downstream signalling pathways such as NF-κB and by this activates pro-inflammatory cytokines ([[TNF]], [[Interleukin 23|IL-23]], [[Interleukin 6|IL-6]], [[Il-2|IL-2]]) and an anti-inflammatory cytokine ([[Interleukin 10|IL-10]]) and subsequently an appropriate innate and adaptive immune response for the efficient clearance of the infection.<ref name="pmid16862125">{{cite journal | vauthors = Gross O, Gewies A, Finger K, Schäfer M, Sparwasser T, Peschel C, Förster I, Ruland J | title = Card9 controls a non-TLR signalling pathway for innate anti-fungal immunity | journal = Nature | volume = 442 | issue = 7103 | pages = 651–6  | date = Aug 2006 | pmid = 16862125 | pmc =  | doi = 10.1038/nature04926 }}</ref>
In 2006, it became clear that Card9 plays important roles within the innate immune respons against yeasts. Card9 mediates signals from so called pattern recognition receptors ([[CLEC7A|Dectin-1]]) to downstream signalling pathways such as [[NF-κB]] and by this activates pro-inflammatory cytokines ([[TNF]], [[Interleukin 23|IL-23]], [[Interleukin 6|IL-6]], [[Il-2|IL-2]]) and an anti-inflammatory cytokine ([[Interleukin 10|IL-10]]) and subsequently an appropriate innate and adaptive immune response to clear an infection.<ref name="pmid16862125">{{cite journal | vauthors = Gross O, Gewies A, Finger K, Schäfer M, Sparwasser T, Peschel C, Förster I, Ruland J | title = Card9 controls a non-TLR signalling pathway for innate anti-fungal immunity | journal = Nature | volume = 442 | issue = 7103 | pages = 651–6  | date = Aug 2006 | pmid = 16862125 | pmc =  | doi = 10.1038/nature04926 }}</ref>
Importantly, it was reported that an autosomal recessive form of susceptibility to chronic mucocutaneous [[candidiasis]] is associated with homozygous mutations in CARD9.<ref name="pmid19864672
An autosomal recessive form of susceptibility to chronic mucocutaneous [[candidiasis]] was found in 2009 to be associated with homozygous mutations in CARD9.<ref name="pmid19864672"> {{cite journal | vauthors = Glocker EO, Hennigs A, Nabavi M, Schäffer AA, Woellner C, Salzer U, Pfeifer D, Veelken H, Warnatz K, Tahami F, Jamal S, Manguiat A, Rezaei N, Amirzargar AA, Plebani A, Hannesschläger N, Gross O, Ruland J, Grimbacher B | title = A homozygous CARD9 mutation in a family with susceptibility to fungal infections | journal = N. Engl. J. Med. | volume = 361 | issue = 18 | pages = 1727–35  | date = Oct 2009 | pmid = 19864672 | pmc = 2793117 | doi = 10.1056/NEJMoa0810719 }}</ref>
">{{cite journal | vauthors = Glocker EO, Hennigs A, Nabavi M, Schäffer AA, Woellner C, Salzer U, Pfeifer D, Veelken H, Warnatz K, Tahami F, Jamal S, Manguiat A, Rezaei N, Amirzargar AA, Plebani A, Hannesschläger N, Gross O, Ruland J, Grimbacher B | title = A homozygous CARD9 mutation in a family with susceptibility to fungal infections | journal = N. Engl. J. Med. | volume = 361 | issue = 18 | pages = 1727–35  | date = Oct 2009 | pmid = 19864672 | pmc = 2793117 | doi = 10.1056/NEJMoa0810719 }}</ref>
Deep dermatophytosis and Card9 deficiency reported in an Iranian family led to its discovery in 17 people from Tunisian, Algerian, and Moroccan families with [[deep dermatophytosis]].<ref>Lanternier F, Pathan S, etal [Deep dermatophytosis and inherited CARD9 deficiency. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4084693/] N Engl J Med. 2013 Oct 31;369(18):1704-1714. doi: 10.1056/NEJMoa1208487.PMID: 24131138</ref>  
Mutations in this gene have been associated to inflammatory diseases such as [[Ankylosing spondylitis]] and [[inflammatory bowel disease]] (Crohn's Disease and Ulcerative Colitis).<ref name="pmid21743469">{{cite journal | vauthors = Evans DM, Spencer CC, Pointon JJ, Su Z, Harvey D, Kochan G, Oppermann U, Opperman U, Dilthey A, Pirinen M, Stone MA, Appleton L, Moutsianas L, Moutsianis L, Leslie S, Wordsworth T, Kenna TJ, Karaderi T, Thomas GP, Ward MM, Weisman MH, Farrar C, Bradbury LA, Danoy P, Inman RD, Maksymowych W, Gladman D, Rahman P, Morgan A, Marzo-Ortega H, Bowness P, Gaffney K, Gaston JS, Smith M, Bruges-Armas J, Couto AR, Sorrentino R, Paladini F, Ferreira MA, Xu H, Liu Y, Jiang L, Lopez-Larrea C, Díaz-Peña R, López-Vázquez A, Zayats T, Band G, Bellenguez C, Blackburn H, Blackwell JM, Bramon E, Bumpstead SJ, Casas JP, Corvin A, Craddock N, Deloukas P, Dronov S, Duncanson A, Edkins S, Freeman C, Gillman M, Gray E, Gwilliam R, Hammond N, Hunt SE, Jankowski J, Jayakumar A, Langford C, Liddle J, Markus HS, Mathew CG, McCann OT, McCarthy MI, Palmer CN, Peltonen L, Plomin R, Potter SC, Rautanen A, Ravindrarajah R, Ricketts M, Samani N, Sawcer SJ, Strange A, Trembath RC, Viswanathan AC, Waller M, Weston P, Whittaker P, Widaa S, Wood NW, McVean G, Reveille JD, Wordsworth BP, Brown MA, Donnelly P | display-authors = 6 | title = Interaction between ERAP1 and HLA-B27 in ankylosing spondylitis implicates peptide handling in the mechanism for HLA-B27 in disease susceptibility | journal = Nat. Genet. | volume = 43 | issue = 8 | pages = 761–7  | date = August 2011 | pmid = 21743469 | doi = 10.1038/ng.873 }}</ref><ref name="pmid21983784">{{cite journal | vauthors = Rivas MA, Beaudoin M, Gardet A, Stevens C, Sharma Y, Zhang CK, Boucher G, Ripke S, Ellinghaus D, Burtt N, Fennell T, Kirby A, Latiano A, Goyette P, Green T, Halfvarson J, Haritunians T, Korn JM, Kuruvilla F, Lagacé C, Neale B, Lo KS, Schumm P, Törkvist L, Dubinsky MC, Brant SR, Silverberg MS, Duerr RH, Altshuler D, Gabriel S, Lettre G, Franke A, D'Amato M, McGovern DP, Cho JH, Rioux JD, Xavier RJ, Daly MJ | title = Deep resequencing of GWAS loci identifies independent rare variants associated with inflammatory bowel disease | journal = Nat. Genet. | volume = 43 | issue = 11 | pages = 1066–73  | date = November 2011 | pmid = 21983784 | pmc = 3378381 | doi = 10.1038/ng.952 }}</ref>


== Interactions ==
CARD9 mutations have been associated with inflammatory diseases such as [[ankylosing spondylitis]] and [[inflammatory bowel disease]] (Crohn's Disease and Ulcerative Colitis).<ref name="pmid21743469">{{cite journal | vauthors = Evans DM, Spencer CC, Pointon JJ, Su Z, Harvey D, Kochan G, Oppermann U, Opperman U, Dilthey A, Pirinen M, Stone MA, Appleton L, Moutsianas L, Moutsianis L, Leslie S, Wordsworth T, Kenna TJ, Karaderi T, Thomas GP, Ward MM, Weisman MH, Farrar C, Bradbury LA, Danoy P, Inman RD, Maksymowych W, Gladman D, Rahman P, Morgan A, Marzo-Ortega H, Bowness P, Gaffney K, Gaston JS, Smith M, Bruges-Armas J, Couto AR, Sorrentino R, Paladini F, Ferreira MA, Xu H, Liu Y, Jiang L, Lopez-Larrea C, Díaz-Peña R, López-Vázquez A, Zayats T, Band G, Bellenguez C, Blackburn H, Blackwell JM, Bramon E, Bumpstead SJ, Casas JP, Corvin A, Craddock N, Deloukas P, Dronov S, Duncanson A, Edkins S, Freeman C, Gillman M, Gray E, Gwilliam R, Hammond N, Hunt SE, Jankowski J, Jayakumar A, Langford C, Liddle J, Markus HS, Mathew CG, McCann OT, McCarthy MI, Palmer CN, Peltonen L, Plomin R, Potter SC, Rautanen A, Ravindrarajah R, Ricketts M, Samani N, Sawcer SJ, Strange A, Trembath RC, Viswanathan AC, Waller M, Weston P, Whittaker P, Widaa S, Wood NW, McVean G, Reveille JD, Wordsworth BP, Brown MA, Donnelly P | display-authors = 6 | title = Interaction between ERAP1 and HLA-B27 in ankylosing spondylitis implicates peptide handling in the mechanism for HLA-B27 in disease susceptibility | journal = Nat. Genet. | volume = 43 | issue = 8 | pages = 761–7  | date = August 2011 | pmid = 21743469 | doi = 10.1038/ng.873 | pmc=3640413}}</ref><ref name="pmid21983784">{{cite journal | vauthors = Rivas MA, Beaudoin M, Gardet A, Stevens C, Sharma Y, Zhang CK, Boucher G, Ripke S, Ellinghaus D, Burtt N, Fennell T, Kirby A, Latiano A, Goyette P, Green T, Halfvarson J, Haritunians T, Korn JM, Kuruvilla F, Lagacé C, Neale B, Lo KS, Schumm P, Törkvist L, Dubinsky MC, Brant SR, Silverberg MS, Duerr RH, Altshuler D, Gabriel S, Lettre G, Franke A, D'Amato M, McGovern DP, Cho JH, Rioux JD, Xavier RJ, Daly MJ | title = Deep resequencing of GWAS loci identifies independent rare variants associated with inflammatory bowel disease | journal = Nat. Genet. | volume = 43 | issue = 11 | pages = 1066–73 | date = November 2011 | pmid = 21983784 | pmc = 3378381 | doi = 10.1038/ng.952 }}</ref>
 
CARD9 has been shown to [[Protein-protein interaction|interact]] with [[BCL10]].<ref name=autogenerated1>{{cite journal | vauthors = Bertin J, Guo Y, Wang L, Srinivasula SM, Jacobson MD, Poyet JL, Merriam S, Du MQ, Dyer MJ, Robison KE, DiStefano PS, Alnemri ES | title = CARD9 is a novel caspase recruitment domain-containing protein that interacts with BCL10/CLAP and activates NF-kappa B | journal = J. Biol. Chem. | volume = 275 | issue = 52 | pages = 41082–6 | date = December 2000 | pmid = 11053425 | doi = 10.1074/jbc.C000726200 }}</ref>


==Model organisms==
==Model organisms==

Revision as of 06:40, 22 June 2018

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Identifiers
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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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Caspase recruitment domain-containing protein 9 is an adaptor protein which in humans is encoded by the CARD9 gene.[1][2]It mediates signals from pattern recognition receptors to activate pro-inflammatory and anti-inflammatory cytokines, regulating inflammation and cell apoptosis. Homozygous mutations in CARD9 are associated with defective innate immunity against yeasts, like Candida and dermatophytes.

Function

CARD9 is a member of the CARD protein family, which is defined by the presence of a characteristic caspase-associated recruitment domain (CARD). CARD is a protein interaction domain known to participate in activation or suppression of CARD containing members of the caspase family, and thus plays an important regulatory role in cell apoptosis. This protein was identified by its selective association with the CARD domain of BCL10, a positive regulator of apoptosis and NF-κB activation.[3]It is thought to function as a molecular scaffold for the assembly of a BCL10 signaling complex that activates NF-κB. Several alternatively spliced transcript variants have been observed, but their full-length nature is not clearly defined.[2]

Clinical significance

In 2006, it became clear that Card9 plays important roles within the innate immune respons against yeasts. Card9 mediates signals from so called pattern recognition receptors (Dectin-1) to downstream signalling pathways such as NF-κB and by this activates pro-inflammatory cytokines (TNF, IL-23, IL-6, IL-2) and an anti-inflammatory cytokine (IL-10) and subsequently an appropriate innate and adaptive immune response to clear an infection.[4] An autosomal recessive form of susceptibility to chronic mucocutaneous candidiasis was found in 2009 to be associated with homozygous mutations in CARD9.[5] Deep dermatophytosis and Card9 deficiency reported in an Iranian family led to its discovery in 17 people from Tunisian, Algerian, and Moroccan families with deep dermatophytosis.[6]

CARD9 mutations have been associated with inflammatory diseases such as ankylosing spondylitis and inflammatory bowel disease (Crohn's Disease and Ulcerative Colitis).[7][8]

Model organisms

Model organisms have been used in the study of CARD9 function. A conditional knockout mouse line called Card9tm1a(EUCOMM)Hmgu was generated at the Wellcome Trust Sanger Institute.[9] Male and female animals underwent a standardized phenotypic screen[10] to determine the effects of deletion.[11][12][13][14] Additional screens performed: - In-depth immunological phenotyping[15] - in-depth bone and cartilage phenotyping[16]

References

  1. ↑ Bertin J, Guo Y, Wang L, Srinivasula SM, Jacobson MD, Poyet JL, Merriam S, Du MQ, Dyer MJ, Robison KE, DiStefano PS, Alnemri ES (Jan 2001). "CARD9 is a novel caspase recruitment domain-containing protein that interacts with BCL10/CLAP and activates NF-kappa B". J. Biol. Chem. 275 (52): 41082–6. doi:10.1074/jbc.C000726200. PMID 11053425.
  2. ↑ 2.0 2.1 "Entrez Gene: CARD9 caspase recruitment domain family, member 9".
  3. ↑ Bertin J, Guo Y, Wang L, Srinivasula SM, Jacobson MD, Poyet JL, Merriam S, Du MQ, Dyer MJ, Robison KE, DiStefano PS, Alnemri ES (December 2000). "CARD9 is a novel caspase recruitment domain-containing protein that interacts with BCL10/CLAP and activates NF-kappa B". J. Biol. Chem. 275 (52): 41082–6. doi:10.1074/jbc.C000726200. PMID 11053425.
  4. ↑ Gross O, Gewies A, Finger K, Schäfer M, Sparwasser T, Peschel C, Förster I, Ruland J (Aug 2006). "Card9 controls a non-TLR signalling pathway for innate anti-fungal immunity". Nature. 442 (7103): 651–6. doi:10.1038/nature04926. PMID 16862125.
  5. ↑ Glocker EO, Hennigs A, Nabavi M, Schäffer AA, Woellner C, Salzer U, Pfeifer D, Veelken H, Warnatz K, Tahami F, Jamal S, Manguiat A, Rezaei N, Amirzargar AA, Plebani A, Hannesschläger N, Gross O, Ruland J, Grimbacher B (Oct 2009). "A homozygous CARD9 mutation in a family with susceptibility to fungal infections". N. Engl. J. Med. 361 (18): 1727–35. doi:10.1056/NEJMoa0810719. PMC 2793117. PMID 19864672.
  6. ↑ Lanternier F, Pathan S, etal [Deep dermatophytosis and inherited CARD9 deficiency. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4084693/] N Engl J Med. 2013 Oct 31;369(18):1704-1714. doi: 10.1056/NEJMoa1208487.PMID: 24131138
  7. ↑ Evans DM, Spencer CC, Pointon JJ, Su Z, Harvey D, Kochan G, et al. (August 2011). "Interaction between ERAP1 and HLA-B27 in ankylosing spondylitis implicates peptide handling in the mechanism for HLA-B27 in disease susceptibility". Nat. Genet. 43 (8): 761–7. doi:10.1038/ng.873. PMC 3640413. PMID 21743469.
  8. ↑ Rivas MA, Beaudoin M, Gardet A, Stevens C, Sharma Y, Zhang CK, Boucher G, Ripke S, Ellinghaus D, Burtt N, Fennell T, Kirby A, Latiano A, Goyette P, Green T, Halfvarson J, Haritunians T, Korn JM, Kuruvilla F, Lagacé C, Neale B, Lo KS, Schumm P, Törkvist L, Dubinsky MC, Brant SR, Silverberg MS, Duerr RH, Altshuler D, Gabriel S, Lettre G, Franke A, D'Amato M, McGovern DP, Cho JH, Rioux JD, Xavier RJ, Daly MJ (November 2011). "Deep resequencing of GWAS loci identifies independent rare variants associated with inflammatory bowel disease". Nat. Genet. 43 (11): 1066–73. doi:10.1038/ng.952. PMC 3378381. PMID 21983784.
  9. ↑ Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
  10. ↑ 10.0 10.1 "International Mouse Phenotyping Consortium".
  11. ↑ 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.
  12. ↑ Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  13. ↑ 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.
  14. ↑ White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Sanger Institute Mouse Genetics Project, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell. 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.
  15. ↑ 15.0 15.1 "Infection and Immunity Immunophenotyping (3i) Consortium".
  16. ↑ "OBCD Consortium".

External links

Further reading

  • Yang H, Minamishima YA, Yan Q, Schlisio S, Ebert BL, Zhang X, Zhang L, Kim WY, Olumi AF, Kaelin WG (2007). "pVHL acts as an adaptor to promote the inhibitory phosphorylation of the NF-kappaB agonist Card9 by CK2". Mol. Cell. 28 (1): 15–27. doi:10.1016/j.molcel.2007.09.010. PMC 2128776. PMID 17936701.
  • Hsu YM, Zhang Y, You Y, Wang D, Li H, Duramad O, Qin XF, Dong C, Lin X (2007). "The adaptor protein CARD9 is required for innate immune responses to intracellular pathogens". Nat. Immunol. 8 (2): 198–205. doi:10.1038/ni1426. PMID 17187069.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  • Wang L, Guo Y, Huang WJ, Ke X, Poyet JL, Manji GA, Merriam S, Glucksmann MA, DiStefano PS, Alnemri ES, Bertin J (2001). "Card10 is a novel caspase recruitment domain/membrane-associated guanylate kinase family member that interacts with BCL10 and activates NF-kappa B". J. Biol. Chem. 276 (24): 21405–9. doi:10.1074/jbc.M102488200. PMID 11259443.
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