|PROSITE documentation PDOC50209 [for PROSITE entry PS50209]|
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 . Recently, it was shown that this domain is widespread among apoptotic signaling molecules and a function in caspase-recruitment has been proposed . 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 .
Important members of the CARD family occur in the following proteins:
December 2001 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Duan H., Dixit V.M.|
|Title||RAIDD is a new 'death' adaptor molecule.|
|2||Authors||Hofmann K., Bucher P., Tschopp J.|
|Title||The CARD domain: a new apoptotic signalling motif.|
|Source||Trends Biochem. Sci. 22:155-156(1997).|
|3||Authors||Chinnaiyan A.M., Chaudhary D., O'Rourke K., Koonin E.V., Dixit V.M.|
|Title||Role of CED-4 in the activation of CED-3.|
|4||Authors||Irmler M., Hofmann K., Vaux D., Tschopp J.|
|Title||Direct physical interaction between the Caenorhabditis elegans 'death proteins' CED-3 and CED-4.|
|Source||FEBS Lett. 406:189-190(1997).|