Caspase-mediated cleavage and DNase activity of the translation initiation factor 3, subunit G (eIF3g)

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dc.contributor.authorJong-Tae Kim-
dc.contributor.authorSeon-Jin Lee-
dc.contributor.authorBo Yeon Kim-
dc.contributor.authorChul Ho Lee-
dc.contributor.authorYoung Il Yeom-
dc.contributor.authorYong Kyung Choe-
dc.contributor.authorD Y Yoon-
dc.contributor.authorS K Chae-
dc.contributor.authorJ W Kim-
dc.contributor.authorY Yang-
dc.contributor.authorJ S Lim-
dc.contributor.authorHee Gu Lee-
dc.date.accessioned2017-04-19T09:45:19Z-
dc.date.available2017-04-19T09:45:19Z-
dc.date.issued2013-
dc.identifier.issn0014-5793-
dc.identifier.uri10.1016/j.febslet.2013.09.027ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/11584-
dc.description.abstractEukaryotic translation initiation factor 3 is composed of 13 subunits (eIF3a through eIF3m) and plays an essential role in translation. During apoptosis, several caspases rapidly down-regulate protein synthesis by cleaving eIF4G, -4B, -3j, and -2α. In this study, we found that the activation of caspases by cisplatin in T24 cells induces the cleavage of subunit G of the eIF3 complex (eIF3g). The cleavage site (SLRD220G) was identified, and we found that the cleaved N-terminus was translocated to the nucleus, activating caspase-3, and that it also showed a strong DNase activity. These data demonstrate the important roles of eIF3g in the translation initiation machinery and in DNA degradation during apoptosis.-
dc.publisherWiley-
dc.titleCaspase-mediated cleavage and DNase activity of the translation initiation factor 3, subunit G (eIF3g)-
dc.title.alternativeCaspase-mediated cleavage and DNase activity of the translation initiation factor 3, subunit G (eIF3g)-
dc.typeArticle-
dc.citation.titleFEBS Letters-
dc.citation.number22-
dc.citation.endPage3674-
dc.citation.startPage3668-
dc.citation.volume587-
dc.contributor.affiliatedAuthorJong-Tae Kim-
dc.contributor.affiliatedAuthorSeon-Jin Lee-
dc.contributor.affiliatedAuthorBo Yeon Kim-
dc.contributor.affiliatedAuthorChul Ho Lee-
dc.contributor.affiliatedAuthorYoung Il Yeom-
dc.contributor.affiliatedAuthorYong Kyung Choe-
dc.contributor.affiliatedAuthorHee Gu Lee-
dc.contributor.alternativeName김종태-
dc.contributor.alternativeName이선진-
dc.contributor.alternativeName김보연-
dc.contributor.alternativeName이철호-
dc.contributor.alternativeName염영일-
dc.contributor.alternativeName최용경-
dc.contributor.alternativeName윤도영-
dc.contributor.alternativeName채선기-
dc.contributor.alternativeName김정우-
dc.contributor.alternativeName양영-
dc.contributor.alternativeName임종석-
dc.contributor.alternativeName이희구-
dc.identifier.bibliographicCitationFEBS Letters, vol. 587, no. 22, pp. 3668-3674-
dc.identifier.doi10.1016/j.febslet.2013.09.027-
dc.subject.keywordApoptosis-
dc.subject.keywordCaspase-
dc.subject.keywordDNase-
dc.subject.keywordeIF3g-
dc.subject.keywordTranslation initiation factor-
dc.subject.localapoptosis-
dc.subject.localApoptosis-
dc.subject.localCaspase-
dc.subject.localCaspases-
dc.subject.localcaspase-
dc.subject.localDNase-
dc.subject.localeIF3g-
dc.subject.localTranslation initiation factor-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Immunotherapy Research Center > 1. Journal Articles
Division of Research on National Challenges > Environmental diseases research center > 1. Journal Articles
Ochang Branch Institute > Chemical Biology Research Center > 1. Journal Articles
Ochang Branch Institute > Division of National Bio-Infrastructure > Laboratory Animal Resource & Research Center > 1. Journal Articles
Division of Biomedical Research > Personalized Genomic Medicine Research Center > 1. Journal Articles
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