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Article: Apoptosis caused by p53-induced protein with death domain (PIDD) depends on the death adapter protein RAIDD

TitleApoptosis caused by p53-induced protein with death domain (PIDD) depends on the death adapter protein RAIDD
Authors
KeywordsCaspase-2
Issue Date2005
Citation
Proceedings of the National Academy of Sciences of the United States of America, 2005, v. 102, n. 40, p. 14314-14320 How to Cite?
AbstractThe p53 tumor suppressor promotes cell cycle arrest or apoptosis in response to diverse stress stimuli. p53-mediated cell death depends in large part on transcriptional up-regulation of target genes. One of these targets, P53-induced protein with a death domain (PIDD), was shown to function as a mediator of p53-dependent apoptosis. Here we show that PIDD is a cytoplasmic protein, and that PIDD-induced apoptosis and growth suppression in embryonic fibroblasts depend on the adaptor protein receptor-interacting protein (RIP)-associated ICH-1/CED-3 homologous protein with a death domain (RAIDD). We provide evidence that PIDD-induced cell death is associated with the early activation of caspase-2 and later activation of caspase-3 and -7. Our results also show that caspase-2-/-, in contrast to RAIDD-/-, mouse embryonic fibroblasts, are only partially resistant to PIDD. Our findings suggest that caspase-2 contributes to PIDD-mediated cell death, but that it is not the sole effector of this pathway. © 2005 by The National Academy of Sciences of the USA.
Persistent Identifierhttp://hdl.handle.net/10722/292545
ISSN
2023 Impact Factor: 9.4
2023 SCImago Journal Rankings: 3.737
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorBerube, Christina-
dc.contributor.authorBoucher, Louis Martin-
dc.contributor.authorMa, Weili-
dc.contributor.authorWakeham, Andrew-
dc.contributor.authorSalmena, Leonardo-
dc.contributor.authorHakem, Razqallah-
dc.contributor.authorYeh, Wen Chen-
dc.contributor.authorMak, Tak W.-
dc.contributor.authorBenchimol, Samuel-
dc.date.accessioned2020-11-17T14:56:42Z-
dc.date.available2020-11-17T14:56:42Z-
dc.date.issued2005-
dc.identifier.citationProceedings of the National Academy of Sciences of the United States of America, 2005, v. 102, n. 40, p. 14314-14320-
dc.identifier.issn0027-8424-
dc.identifier.urihttp://hdl.handle.net/10722/292545-
dc.description.abstractThe p53 tumor suppressor promotes cell cycle arrest or apoptosis in response to diverse stress stimuli. p53-mediated cell death depends in large part on transcriptional up-regulation of target genes. One of these targets, P53-induced protein with a death domain (PIDD), was shown to function as a mediator of p53-dependent apoptosis. Here we show that PIDD is a cytoplasmic protein, and that PIDD-induced apoptosis and growth suppression in embryonic fibroblasts depend on the adaptor protein receptor-interacting protein (RIP)-associated ICH-1/CED-3 homologous protein with a death domain (RAIDD). We provide evidence that PIDD-induced cell death is associated with the early activation of caspase-2 and later activation of caspase-3 and -7. Our results also show that caspase-2-/-, in contrast to RAIDD-/-, mouse embryonic fibroblasts, are only partially resistant to PIDD. Our findings suggest that caspase-2 contributes to PIDD-mediated cell death, but that it is not the sole effector of this pathway. © 2005 by The National Academy of Sciences of the USA.-
dc.languageeng-
dc.relation.ispartofProceedings of the National Academy of Sciences of the United States of America-
dc.subjectCaspase-2-
dc.titleApoptosis caused by p53-induced protein with death domain (PIDD) depends on the death adapter protein RAIDD-
dc.typeArticle-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1073/pnas.0506475102-
dc.identifier.pmid16183742-
dc.identifier.pmcidPMC1242316-
dc.identifier.scopuseid_2-s2.0-26444433872-
dc.identifier.volume102-
dc.identifier.issue40-
dc.identifier.spage14314-
dc.identifier.epage14320-
dc.identifier.isiWOS:000232392900036-
dc.identifier.issnl0027-8424-

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