The PIDDosome, a Protein Complex Implicated in Activation of Caspase-2 in Response to Genotoxic Stress

By A. Tinel, J. Tschopp. Science, 2004

682 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/b6b8f803418b6bd42f1953ca59afc14893bf2afb

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. Simone Fulda
2. T. Kanneganti
3. K. Debatin
4. Douglas R. Green
5. F. Llambi
6. Junying Yuan
7. R. Malireddi
8. S. Kesavardhana

In Oncology

1. Simone Fulda
2. K. Debatin
3. M. Karin
4. Sharad Kumar
5. J. Li
6. Douglas R. Green
7. Junying Yuan
8. T. Mak

Citations in the corpus

• Caspase function in programmed cell death (2007, background): “Caspase-2 is recruited into a protein complex similar to the Apaf-1/caspase-9 apoptosome.101 The adaptor proteins RAIDD and PIDD have been identified as members of this large complex designated the ‘PIDDosome’.101 An unusual feature of caspase-2 is its localisation to the nucleus and the Golgi in ad”
• Caspase functions in cell death and disease. (2013, background): “DNA-PKcs-PIDDosome: A nuclear caspase-2-activating complex with role in G2/M checkpoint maintenance.”
• Caspases in apoptosis and beyond (2008, background): “A large protein complex, named PIDDosome, that contains the p53-induced protein with a death domain (PIDD) and an adapter protein RAIDD, has been shown to mediate the activation of caspase-2 in response to genotoxic stimuli (Tinel and Tschopp, 2004).”
• Regulation and Function of IKK and IKK-Related Kinases (2006, background): “Sumoylation of IKKγ is increased in cells overexpressing PIDD (p53-induced protein with a death domain), a p53-inducible protein that was originally described as a proapoptotic molecule (159, 160).”
• Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy (2006, background): “Upon DNA damage, caspase-2 has recently been reported to become activated in the socalled PIDDosome, a complex of the p53-inducible, death domain-containing protein PIDD, caspase-2 and the adaptor protein RAIDD (Tinel and Tschopp, 2004) pointing to the existence of a nucleo-mitochondrial apoptotic p”
• Caspases in Cell Death, Inflammation, and Gasdermin-Induced Pyroptosis (2020, background): “Caspase-2 is activated in PIDDosome in response to genotoxic stress and failure of cytokinesis to inhibit cell proliferation (11, 12).”
• Cell Death Signaling. (2015, background): “This allows the binding of 14-3-3z, which prevents association with the PIDDosome (Nutt et al. 2009).”
• Cellular mechanisms controlling caspase activation and function. (2013, background): “The current model for caspase-2 activation involves two adaptor proteins, PIDD (p53-induced protein with a death domain) and RAIDD (RIP-associated ICH-1/CED-3 homologous proteins with a death domain) (Duan and Dixit 1997; Read et al. 2002; Tinel and Tschopp 2004).”