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Article: Posttranscriptional downregulation of c-IAP2 by the ubiquitin protein ligase c-IAP1 in vivo

TitlePosttranscriptional downregulation of c-IAP2 by the ubiquitin protein ligase c-IAP1 in vivo
Authors
Issue Date2005
Citation
Molecular and Cellular Biology, 2005, v. 25, n. 8, p. 3348-3356 How to Cite?
AbstractInhibitor of apoptosis proteins (IAPs) c-IAP1 and C-IAP2 were identified as part of the tumor necrosis factor receptor 2 (TNFR2) signaling complex and have been implicated as intermediaries in tumor necrosis factor alpha signaling. Like all RING domain-containing IAPs, c-IAP1 and C-IAP2 have ubiquitin protein ligase (E3) activity. To explore the function of c-IAP1 in a physiologic setting, c-IAP1-deficient mice were generated by homologous gene recombination. These animals are viable and have no obvious sensitization to proapoptotic stimuli. Cells from c-IAP1-/- mice do, however, express markedly elevated levels of C-IAP2 protein in the absence of increased C-IAP2 mRNA. In contrast to reports implicating c-IAPs in the activation of NF-κB, resting and cytokine-induced NF-κB activation was not impaired in c-IAP1-deficient cells. Transient transfection studies with wild-type and E3-defective c-IAP1 revealed that C-IAP2 is a direct target for c-IAP1-mediated ubiquitination and subsequent degradation, which are potentiated by the adaptor function of TRAF2. Thus, the c-IAPs represent a pair of TNFR-associated ubiquitin protein ligases in which one regulates the expression of the other by a posttranscriptional and E3-dependent mechanism. Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Persistent Identifierhttp://hdl.handle.net/10722/291705
ISSN
2023 Impact Factor: 3.2
2023 SCImago Journal Rankings: 1.452
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorConze, Dietrich B.-
dc.contributor.authorAlbert, Lori-
dc.contributor.authorFerrick, David A.-
dc.contributor.authorGoeddel, David V.-
dc.contributor.authorYeh, Wen Chen-
dc.contributor.authorMak, Tak-
dc.contributor.authorAshwell, Jonathan D.-
dc.date.accessioned2020-11-17T14:54:56Z-
dc.date.available2020-11-17T14:54:56Z-
dc.date.issued2005-
dc.identifier.citationMolecular and Cellular Biology, 2005, v. 25, n. 8, p. 3348-3356-
dc.identifier.issn0270-7306-
dc.identifier.urihttp://hdl.handle.net/10722/291705-
dc.description.abstractInhibitor of apoptosis proteins (IAPs) c-IAP1 and C-IAP2 were identified as part of the tumor necrosis factor receptor 2 (TNFR2) signaling complex and have been implicated as intermediaries in tumor necrosis factor alpha signaling. Like all RING domain-containing IAPs, c-IAP1 and C-IAP2 have ubiquitin protein ligase (E3) activity. To explore the function of c-IAP1 in a physiologic setting, c-IAP1-deficient mice were generated by homologous gene recombination. These animals are viable and have no obvious sensitization to proapoptotic stimuli. Cells from c-IAP1-/- mice do, however, express markedly elevated levels of C-IAP2 protein in the absence of increased C-IAP2 mRNA. In contrast to reports implicating c-IAPs in the activation of NF-κB, resting and cytokine-induced NF-κB activation was not impaired in c-IAP1-deficient cells. Transient transfection studies with wild-type and E3-defective c-IAP1 revealed that C-IAP2 is a direct target for c-IAP1-mediated ubiquitination and subsequent degradation, which are potentiated by the adaptor function of TRAF2. Thus, the c-IAPs represent a pair of TNFR-associated ubiquitin protein ligases in which one regulates the expression of the other by a posttranscriptional and E3-dependent mechanism. Copyright © 2005, American Society for Microbiology. All Rights Reserved.-
dc.languageeng-
dc.relation.ispartofMolecular and Cellular Biology-
dc.titlePosttranscriptional downregulation of c-IAP2 by the ubiquitin protein ligase c-IAP1 in vivo-
dc.typeArticle-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1128/MCB.25.8.3348-3356.2005-
dc.identifier.pmid15798218-
dc.identifier.pmcidPMC1069614-
dc.identifier.scopuseid_2-s2.0-16244377737-
dc.identifier.volume25-
dc.identifier.issue8-
dc.identifier.spage3348-
dc.identifier.epage3356-
dc.identifier.isiWOS:000228138500041-
dc.identifier.issnl0270-7306-

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