The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

CRADD  -  CASP2 and RIPK1 domain containing adaptor...

Homo sapiens

Synonyms: Caspase and RIP adapter with death domain, Death domain-containing protein CRADD, MRT34, RAIDD, RIP-associated protein with a death domain
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on CRADD

  • We have solved the CARD structure of the RAIDD adaptor protein that recruits ICH-1/caspase-2 [1].
  • Here we describe such an adaptor molecule, RAIDD, which has an unusual bipartite architecture comprising a carboxy-terminal death domain that binds to the homologous domain in RIP, a serine/threonine kinase component of the death pathway [2].
  • Apaf-1 CARD consists of six tightly packed amphipathic alpha-helices and is topologically similar to the RAIDD CARD, with the exception of a kink observed in the middle of the N-terminal helix [3].
  • RAIDD localization is not affected by TNF-treatment of HeLa cells, but in cells ectopically expressing caspase-2, a fraction of RAIDD is recruited to the nucleus [4].
  • CRADD has a dual-domain structure similar to that of FADD [5].

Biological context of CRADD

  • Another DD-containing adaptor/signaling molecule, CRADD, was identified and was shown to induce apoptosis [5].
  • In support of these observations we found that Bcl-2 and Bcl-xL can block caspase-2- and CRADD (caspase and RIP adaptor with death domain)-induced cell death [6].
  • Mutagenesis data suggest that these patches mediate CARD/CARD interaction between RAIDD and ICH-1 [1].
  • This assumption was further supported by siRNA transfections targeting PIDD or RAIDD [7].

Associations of CRADD with chemical compounds

  • In this study we compare the thermodynamic, folding and stability properties of different members of the PAAD and CARD families and investigate structural conformational changes induced by the helix inducers trifluoroethanol and SDS on the PAAD domain of IFI16 and on the CARD domain of RAIDD [8].

Physical interactions of CRADD

  • RAIDD has an N-terminal caspase recruitment domain (CARD) that interacts with the CARD of caspase-2 and a C-terminal death domain (DD) that interacts with the DD in PIDD [9].
  • RIP also recruits caspase-2 to the TNFR-1 signaling complex via the adaptor protein RAIDD, which contains a DD and a caspase-recruiting domain (CARD) [10].

Other interactions of CRADD

  • CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP [5].
  • We show that activation of caspase-2 occurs in a complex that contains the death domain-containing protein PIDD, whose expression is induced by p53, and the adaptor protein RAIDD [11].
  • This interaction surface is distinct from that proposed based on the structure of the CARD from RAIDD, but is coincident with that of the structurally similar FADD death effector domain and the Apaf-1 CARD interface identified by crystallographic studies [12].
  • The expression levels of CDKN2C, CRADD, and IGFBP-2 genes were significantly associated with the event-free survival of the patients in AML [13].
  • Here we provide evidence that CED-3 and CED-4 both contain sequences with homology to a domain present in RAIDD and the prodomain of certain ICE-like proteases (caspases) [14].


  1. Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment. Chou, J.J., Matsuo, H., Duan, H., Wagner, G. Cell (1998) [Pubmed]
  2. RAIDD is a new 'death' adaptor molecule. Duan, H., Dixit, V.M. Nature (1997) [Pubmed]
  3. Solution structure of Apaf-1 CARD and its interaction with caspase-9 CARD: a structural basis for specific adaptor/caspase interaction. Zhou, P., Chou, J., Olea, R.S., Yuan, J., Wagner, G. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  4. Subcellular localization and CARD-dependent oligomerization of the death adaptor RAIDD. Shearwin-Whyatt, L.M., Harvey, N.L., Kumar, S. Cell Death Differ. (2000) [Pubmed]
  5. CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP. Ahmad, M., Srinivasula, S.M., Wang, L., Talanian, R.V., Litwack, G., Fernandes-Alnemri, T., Alnemri, E.S. Cancer Res. (1997) [Pubmed]
  6. Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria. Guo, Y., Srinivasula, S.M., Druilhe, A., Fernandes-Alnemri, T., Alnemri, E.S. J. Biol. Chem. (2002) [Pubmed]
  7. Functional connection between p53 and caspase-2 is essential for apoptosis induced by DNA damage. Vakifahmetoglu, H., Olsson, M., Orrenius, S., Zhivotovsky, B. Oncogene (2006) [Pubmed]
  8. Thermodynamics and stability of the PAAD/DAPIN/PYRIN domain of IFI-16. Dalal, K., Pio, F. FEBS Lett. (2006) [Pubmed]
  9. Crystal structure of RAIDD death domain implicates potential mechanism of PIDDosome assembly. Park, H.H., Wu, H. J. Mol. Biol. (2006) [Pubmed]
  10. Identification of CARDIAK, a RIP-like kinase that associates with caspase-1. Thome, M., Hofmann, K., Burns, K., Martinon, F., Bodmer, J.L., Mattmann, C., Tschopp, J. Curr. Biol. (1998) [Pubmed]
  11. The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress. Tinel, A., Tschopp, J. Science (2004) [Pubmed]
  12. Solution structure and mutagenesis of the caspase recruitment domain (CARD) from Apaf-1. Day, C.L., Dupont, C., Lackmann, M., Vaux, D.L., Hinds, M.G. Cell Death Differ. (1999) [Pubmed]
  13. Identification of novel genes with prognostic value in childhood leukemia using cDNA microarray and quantitative RT-PCR. Hattori, H., Matsuzaki, A., Suminoe, A., Koga, Y., Tashiro, K., Hara, T. Pediatric hematology and oncology. (2006) [Pubmed]
  14. Direct physical interaction between the Caenorhabditis elegans 'death proteins' CED-3 and CED-4. Irmler, M., Hofmann, K., Vaux, D., Tschopp, J. FEBS Lett. (1997) [Pubmed]
WikiGenes - Universities