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PROSITE documentation PDOC50209 [for PROSITE entry PS50209]

CARD caspase recruitment domain profile





Description

The apoptotic signal coming from ligand-induced oligomerization of death receptors is mediated by a number of adaptor proteins containing specialized interaction domains. Besides the caspase recruitment domain (CARD), this group is formed by the death domain (DD) (see <PDOC50017>) and the death effector domain (DED) (see <PDOC50168>).

The CARD domain was first described as a homology region in the N-terminus of the death adaptor protein RAIDD and the caspases ced-3 and CASP2 [1]. Recently, it was shown that this domain is widespread among apoptotic signaling molecules and a function in caspase-recruitment has been proposed [2]. The CARD domain typically associates with other CARD-containing proteins, forming either dimers or trimers [1,2,3,4]. It has been predicted that CARD is related in structure and sequence to both DD and DED domains, which work in similar pathways and show similar interaction properties [2].

Important members of the CARD family occur in the following proteins:

  • RAIDD death adaptor protein [1].
  • Caspases: Ced-3, CASP1, CASP2, CASP4, CASP5, CASP9 and CASP12.
  • Inhibitor of apoptosis (IAP) proteins c-IAP1 and c-IAP2.
  • Caenorhabditis elegans cell death protein ced-4 and its mammalian homologue Apaf-1.
  • Equine herpes virus protein E10.
Expert(s) to contact by email:

Hofmann K.

Last update:

December 2001 / First entry.

Technical section

PROSITE method (with tools and information) covered by this documentation:

CARD, PS50209; CARD caspase recruitment domain profile  (MATRIX)


References

1AuthorsDuan H. Dixit V.M.
TitleRAIDD is a new 'death' adaptor molecule.
SourceNature 385:86-89(1997).
PubMed ID8985253

2AuthorsHofmann K. Bucher P. Tschopp J.
TitleThe CARD domain: a new apoptotic signalling motif.
SourceTrends Biochem. Sci. 22:155-156(1997).
PubMed ID9175472

3AuthorsChinnaiyan A.M. Chaudhary D. O'Rourke K. Koonin E.V. Dixit V.M.
TitleRole of CED-4 in the activation of CED-3.
SourceNature 388:728-729(1997).
PubMed ID9285582
DOI10.1038/41913

4AuthorsIrmler M. Hofmann K. Vaux D. Tschopp J.
TitleDirect physical interaction between the Caenorhabditis elegans 'death proteins' CED-3 and CED-4.
SourceFEBS Lett. 406:189-190(1997).
PubMed ID9109415



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