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CASP2 and RIPK1 domain containing adaptor with death domain

The protein encoded by this gene is a death domain (CARD/DD)-containing protein and has been shown to induce cell apoptosis. Through its CARD domain, this protein interacts with, and thus recruits, caspase 2/ICH1 to the cell death signal transduction complex that includes tumor necrosis factor receptor 1 (TNFR1A), RIPK1/RIP kinase, and numbers of other CARD domain-containing proteins. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: PrP, caspase-2, CAN, p53, caspase-9
Papers on RAIDD
The tumor-modulatory effects of Caspase-2 and Pidd1 do not require the scaffold protein Raidd.
Manzl et al., Innsbruck, Austria. In Cell Death Differ, Nov 2015
The receptor-interacting protein-associated ICH-1/CED-3 homologous protein with a death domain (RAIDD/CRADD) functions as a dual adaptor and is a constituent of different multi-protein complexes implicated in the regulation of inflammation and cell death.
New paradigms in sepsis: from prevention to protection of failing microcirculation.
Zienkiewicz et al., Nashville, United States. In J Thromb Haemost, Oct 2015
inhibitors of NF-κB, A20 protein, CRADD/RAIDD protein and microRNAs) regulate endothelial signaling.
An Inhibitor of PIDDosome Formation.
Sidi et al., New York City, United States. In Mol Cell, Jul 2015
The PIDDosome-PIDD-RAIDD-caspase-2 complex-is a proapoptotic caspase-activation platform of elusive significance.
Flexible stoichiometry and asymmetry of the PIDDosome core complex by heteronuclear NMR spectroscopy and mass spectrometry.
Driscoll et al., London, United Kingdom. In J Mol Biol, Mar 2015
The structure of the PIDDosome core complex exhibits an asymmetric three-layered arrangement containing five PIDD-DDs in one layer, five RAIDD-DDs in a second layer and an additional two RAIDD-DDs.
The adaptor CRADD/RAIDD controls activation of endothelial cells by proinflammatory stimuli.
Hawiger et al., Nashville, United States. In J Biol Chem, 2014
Previously, we reported that BCL10 in immune cells is targeted by the "death" adaptor CRADD/RAIDD (CRADD), which negatively regulates nuclear factor κB (NFκB)-dependent cytokine and chemokine expression in T cells (Lin, Q., Liu, Y., Moore, D. J., Elizer, S. K., Veach, R. A., Hawiger, J., and Ruley, H. E. (2012) J. Immunol.
Regulation of CRADD-caspase 2 cascade by histone deacetylase 1 in gastric cancer.
Wang et al., China. In Am J Transl Res, 2013
CRADD, also referred as RAIDD, is an adaptor protein that could interact with both caspase 2 and RIP that can promote apoptosis once activated.
Caspase-2 is essential for c-Jun transcriptional activation and Bim induction in neuron death.
Troy et al., New York City, United States. In Biochem J, 2013
Caspase-2 activation is dependent on the adaptor protein RAIDD {RIP (receptor-interacting protein)-associated ICH-1 [ICE (interleukin-1β-converting enzyme)/CED-3 (cell-death determining 3) homologue 1] protein with a death domain}, and both caspase-2 and RAIDD are required for c-Jun activation and Bim induction.
PIDD mediates and stabilizes the interaction between RAIDD and caspase-2 for the PIDDosome assembly.
Park et al., Kyŏngsan, South Korea. In Bmb Rep, 2013
The PIDDosome, which is an oligomeric signaling complex composed of PIDD, RAIDD and caspase-2, can induce proximity-based dimerization and activation of caspase-2.
Caspase-2 is involved in cell death induction by taxanes in breast cancer cells.
Kovář et al., In Cancer Cell Int, 2012
The inhibition of RAIDD expression using siRNA did not affect the number of surviving SK-BR-3 and MCF-7 cells after taxane application at all.
Neuronal caspase 2 activity and function requires RAIDD, but not PIDD.
Troy et al., New York City, United States. In Biochem J, 2012
Neuronal caspase-2-dependent execution of neurons requires recptor-interacting protein RAIDD, not p53-inducible protein with a death domain (PIDD).
Cutting edge: the "death" adaptor CRADD/RAIDD targets BCL10 and suppresses agonist-induced cytokine expression in T lymphocytes.
Ruley et al., Nashville, United States. In J Immunol, 2012
We show that CRADD interacts with BCL10 through its caspase recruitment domain and suppresses interactions between BCL10 and CARMA1
Genetic mapping and exome sequencing identify variants associated with five novel diseases.
Strauss et al., United States. In Plos One, 2011
Study identified sequence variants in the known disease-causing genes SLC6A3 and FLVCR1, and present evidence to strongly support the pathogenicity of variants identified in TUBGCP6, BRAT1, SNIP1, CRADD, and HARS.
Identification and analysis of dominant negative mutants of RAIDD and PIDD.
Park et al., Kyŏngsan, South Korea. In Biochim Biophys Acta, 2010
point mutations on RAIDD (R147E) and on PIDD (Y814A) exert a dominant negative effect on the formation of the PIDDosome, and that this effect cannot be applied after the PIDDosome has been formed
PIDDosome expression and the role of caspase-2 activation for chemotherapy-induced apoptosis in RCCs.
Mahotka et al., Düsseldorf, Germany. In Cell Oncol, 2009
The expressions of PIDD and RAIDD are upregulated during tumour progression in renal cell carcinomas.
Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex.
Wu et al., New York City, United States. In Cell, 2007
Here we report the crystal structure of the PIDD DD and RAIDD DD complex, which forms the core of the caspase-2-activating complex PIDDosome.
In situ trapping of activated initiator caspases reveals a role for caspase-2 in heat shock-induced apoptosis.
Green et al., San Diego, United States. In Nat Cell Biol, 2006
Furthermore, cells lacking the adapter molecule RAIDD failed to activate caspase-2 after heat shock treatment and showed resistance to apoptosis in this setting.
The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress.
Tschopp et al., Lausanne, Switzerland. In Science, 2004
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.
Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment.
Wagner et al., Cambridge, United States. In Cell, 1998
We have solved the CARD structure of the RAIDD adaptor protein that recruits ICH-1/caspase-2.
Caspases: the executioners of apoptosis.
Cohen, Leicester, United Kingdom. In Biochem J, 1997
The importance of caspase prodomains in the regulation of apoptosis is further highlighted by the recognition of adapter molecules, such as RAIDD [receptor-interacting protein (RIP)-associated ICH-1/CED-3-homologous protein with a death domain]/CRADD (caspase and RIP adapter with death domain), which binds to the prodomain of caspase-2 and recruits it to the signalling complex.
RAIDD is a new 'death' adaptor molecule.
Dixit et al., Ann Arbor, United States. In Nature, 1997
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.
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