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Article: TRADD contributes to tumour suppression by regulating ULF-dependent p19 Arf ubiquitylation

TitleTRADD contributes to tumour suppression by regulating ULF-dependent p19 <sup>Arf</sup> ubiquitylation
Authors
Issue Date2012
Citation
Nature Cell Biology, 2012, v. 14, n. 6, p. 625-633 How to Cite?
AbstractTumour necrosis factor receptor (TNFR)-associated death domain (TRADD) protein is a central adaptor in the TNFR1 signalling complex that mediates both cell death and inflammatory signals. Here, we report that Tradd deficiency in mice accelerated tumour formation in a chemical-induced carcinogenesis model independently of TNFR1 signalling. In vitro, primary cells lacking TRADD were less susceptible to HRas-induced senescence and showed a reduced level of accumulation of the p19 Arf tumour suppressor protein. Our data indicate that TRADD shuttles dynamically from the cytoplasm into the nucleus to modulate the interaction between p19 Arf and its E3 ubiquitin ligase ULF, thereby promoting p19 Arf protein stability and tumour suppression. These results reveal a previously unknown tumour-suppressive role for nuclear TRADD, augmenting its long-established cytoplasmic functions in inflammatory and immune signalling cascades. Our findings also make an important contribution to the rapidly expanding field of p19 Arf post-translational regulation. © 2012 Macmillan Publishers Limited. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/292707
ISSN
2023 Impact Factor: 17.3
2023 SCImago Journal Rankings: 8.913
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorChio, Iok In Christine-
dc.contributor.authorSasaki, Masato-
dc.contributor.authorGhazarian, Danny-
dc.contributor.authorMoreno, Juan-
dc.contributor.authorDone, Susan-
dc.contributor.authorUeda, Takeshi-
dc.contributor.authorInoue, Satoshi-
dc.contributor.authorChang, Yu Ling-
dc.contributor.authorChen, Nien Jung-
dc.contributor.authorMak, Tak Wah-
dc.date.accessioned2020-11-17T14:57:03Z-
dc.date.available2020-11-17T14:57:03Z-
dc.date.issued2012-
dc.identifier.citationNature Cell Biology, 2012, v. 14, n. 6, p. 625-633-
dc.identifier.issn1465-7392-
dc.identifier.urihttp://hdl.handle.net/10722/292707-
dc.description.abstractTumour necrosis factor receptor (TNFR)-associated death domain (TRADD) protein is a central adaptor in the TNFR1 signalling complex that mediates both cell death and inflammatory signals. Here, we report that Tradd deficiency in mice accelerated tumour formation in a chemical-induced carcinogenesis model independently of TNFR1 signalling. In vitro, primary cells lacking TRADD were less susceptible to HRas-induced senescence and showed a reduced level of accumulation of the p19 Arf tumour suppressor protein. Our data indicate that TRADD shuttles dynamically from the cytoplasm into the nucleus to modulate the interaction between p19 Arf and its E3 ubiquitin ligase ULF, thereby promoting p19 Arf protein stability and tumour suppression. These results reveal a previously unknown tumour-suppressive role for nuclear TRADD, augmenting its long-established cytoplasmic functions in inflammatory and immune signalling cascades. Our findings also make an important contribution to the rapidly expanding field of p19 Arf post-translational regulation. © 2012 Macmillan Publishers Limited. All rights reserved.-
dc.languageeng-
dc.relation.ispartofNature Cell Biology-
dc.titleTRADD contributes to tumour suppression by regulating ULF-dependent p19 <sup>Arf</sup> ubiquitylation-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1038/ncb2496-
dc.identifier.pmid22561347-
dc.identifier.scopuseid_2-s2.0-84861592640-
dc.identifier.volume14-
dc.identifier.issue6-
dc.identifier.spage625-
dc.identifier.epage633-
dc.identifier.eissn1476-4679-
dc.identifier.isiWOS:000304599900012-
dc.identifier.issnl1465-7392-

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