CARD14

CARD14
Identifiers
AliasesCARD14, BIMP2, CARMA2, PRP, PSORS2, PSS1, caspase recruitment domain family member 14
External IDsMGI: 2386258 HomoloGene: 11469 GeneCards: CARD14
Orthologs
SpeciesHumanMouse
Entrez

79092

170720

Ensembl

ENSG00000141527

ENSMUSG00000013483

UniProt

Q9BXL6

Q99KF0

RefSeq (mRNA)

NM_001257970
NM_024110
NM_052819

NM_130886

RefSeq (protein)

NP_001244899
NP_077015
NP_438170

NP_570956

Location (UCSC)Chr 17: 80.17 – 80.21 MbChr 11: 119.31 – 119.35 Mb
PubMed search[1][2]
Wikidata
View/Edit HumanView/Edit Mouse

Caspase recruitment domain-containing protein 14, also known as CARD-containing MAGUK protein 2 (Carma 2), is a protein that in humans is encoded by the CARD14 gene.[3][4][5]

Function

The protein encoded by this gene belongs to the membrane-associated guanylate kinase (MAGUK) family, a class of proteins that functions as molecular scaffolds for the assembly of multiprotein complexes at specialized regions of the plasma membrane. This protein is also a member of the CARD protein family, which is defined by carrying a characteristic caspase-associated recruitment domain (CARD). This protein shares a similar domain structure with CARD11 protein. The CARD domains of both proteins have been shown to specifically interact with BCL10, a protein known to function as a positive regulator of cell apoptosis and NF-κB activation. The homotypic interaction with BCL10 is believed to be prevented by the linker region of CARD14, when in an inactive state.[6] CARD14 overexpression leads to an activation of the transcription factor NF-κB and phosphorylation of BCL10. CARD14 has been shown to form a CBM signalosome, similar to the signalling of CARD11, with BCL10 and MALT1.[3][6]

The CARD14 gene was recently identified as the first gene directly linked to the most common form of Psoriasis. It has been suggested that a mutation in the gene plus an environmental trigger were enough to elicit plaque psoriasis.[7][8] These rare, but highly penetrant, mutations were found to disrupt an auto-inhibited state of CARD14, which leads to the binding of BCL10 and the activation of NF-κB.[6]

References

  1. ↑ "Human PubMed Reference:".
  2. ↑ "Mouse PubMed Reference:".
  3. 1 2 "Entrez Gene: caspase recruitment domain family".
  4. ↑ Bertin J, Wang L, Guo Y, Jacobson MD, Poyet JL, Srinivasula SM, Merriam S, DiStefano PS, Alnemri ES (April 2001). "CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-associated guanylate kinase (MAGUK) family members that interact with BCL10 and activate NF-kappa B". J. Biol. Chem. 276 (15): 11877–82. PMID 11278692. doi:10.1074/jbc.M010512200.
  5. ↑ Gaide O, Martinon F, Micheau O, Bonnet D, Thome M, Tschopp J (May 2001). "Carma1, a CARD-containing binding partner of Bcl10, induces Bcl10 phosphorylation and NF-kappaB activation". FEBS Lett. 496 (2–3): 121–7. PMID 11356195. doi:10.1016/S0014-5793(01)02414-0.
  6. 1 2 3 Howes, A; O'Sullivan, PA; Breyer, F; Ghose, A; Cao, L; Krappmann, D; Bowcock, AM; Ley, SC (12 April 2016). "Psoriasis mutations disrupt CARD14 autoinhibition promoting BCL10-MALT1-dependent NF-κB activation". The Biochemical Journal. 473 (12): 1759–68. PMID 27071417. doi:10.1042/BCJ20160270.
  7. ↑ Jordan CT, Cao L, Roberson EDO; et al. (April 19, 2012). "Rare and common variants in CARD14, encoding an epidermal regulator of NF-kappaB, in psoriasis". The American Journal of Human Genetics. 90 (5): 796–808. PMC 3376540 Freely accessible. PMID 22521419. doi:10.1016/j.ajhg.2012.03.013.
  8. ↑ Jordan CT, Cao L, Roberson EDO; et al. (April 19, 2012). "PSORS2 is due to mutations in CARD14". The American Journal of Human Genetics. 90 (5): 784. doi:10.1016/j.ajhg.2012.03.012.

Further reading

  • Wang L, Guo Y, Huang WJ, et al. (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. PMID 11259443. doi:10.1074/jbc.M102488200. 

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


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