cIAPs promote the proteasomal degradation of mutant SOD1 linked to familial amyotrophic lateral sclerosis = 가족성 근위축성 측삭경화증 연관 돌연변이 SOD1 단백질의 cIAP에 의한 분해

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dc.contributor.authorJin Sun Choi-
dc.contributor.authorKidae Kim-
dc.contributor.authorD H Lee-
dc.contributor.authorS Cho-
dc.contributor.authorJ D Ha-
dc.contributor.authorByoung Chul Park-
dc.contributor.authorSunhong Kim-
dc.contributor.authorSung Goo Park-
dc.contributor.authorJeong Hoon Kim-
dc.date.accessioned2017-04-19T10:28:21Z-
dc.date.available2017-04-19T10:28:21Z-
dc.date.issued2016-
dc.identifier.issn0006-291X-
dc.identifier.uri10.1016/j.bbrc.2016.10.065ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/13471-
dc.description.abstractAlthough the ubiquitin?proteasome system is believed to play an important role in the pathogenesis of familial amyotrophic lateral sclerosis (FALS), caused by mutations in Cu/Zn-superoxide dismutase 1 (SOD1), the mechanism of how mutant SOD1 protein is regulated in cells is still poorly understood. Here we have demonstrated that cellular inhibitor of apoptosis proteins (cIAPs) are specifically associated with FALS-linked mutant SOD1 (mSOD1) and that this interaction promotes the ubiquitin-dependent proteasomal degradation of mutant SOD1. By utilizing cumate inducible SOD1 cells, we also showed that knock-down or pharmacologic depletion of cIAPs leads to H2O2 induced cytotoxicity in mSOD1 expressing cells. Altogether, our results reveal a novel role of cIAPs in FALS-associated mutant SOD1 regulation.-
dc.publisherElsevier-
dc.titlecIAPs promote the proteasomal degradation of mutant SOD1 linked to familial amyotrophic lateral sclerosis = 가족성 근위축성 측삭경화증 연관 돌연변이 SOD1 단백질의 cIAP에 의한 분해-
dc.title.alternativecIAPs promote the proteasomal degradation of mutant SOD1 linked to familial amyotrophic lateral sclerosis-
dc.typeArticle-
dc.citation.titleBiochemical and Biophysical Research Communications-
dc.citation.number3-
dc.citation.endPage428-
dc.citation.startPage422-
dc.citation.volume480-
dc.contributor.affiliatedAuthorJin Sun Choi-
dc.contributor.affiliatedAuthorKidae Kim-
dc.contributor.affiliatedAuthorByoung Chul Park-
dc.contributor.affiliatedAuthorSunhong Kim-
dc.contributor.affiliatedAuthorSung Goo Park-
dc.contributor.affiliatedAuthorJeong Hoon Kim-
dc.contributor.alternativeName최진선-
dc.contributor.alternativeName김기대-
dc.contributor.alternativeName이도희-
dc.contributor.alternativeName조사연-
dc.contributor.alternativeName하재두-
dc.contributor.alternativeName박병철-
dc.contributor.alternativeName김선홍-
dc.contributor.alternativeName박성구-
dc.contributor.alternativeName김정훈-
dc.identifier.bibliographicCitationBiochemical and Biophysical Research Communications, vol. 480, no. 3, pp. 422-428-
dc.identifier.doi10.1016/j.bbrc.2016.10.065-
dc.subject.keywordcIAPs-
dc.subject.keywordFALS-
dc.subject.keywordSOD1-
dc.subject.keywordUbiquitination-
dc.subject.localcIAP-
dc.subject.localcIAPs-
dc.subject.localFALS-
dc.subject.localSOD1-
dc.subject.localUbiquitination-
dc.subject.localubiquitination-
dc.description.journalClassY-
Appears in Collections:
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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