Proteasome inhibition induces alpha-synuclein SUMOylation and aggregate formation
DC Field | Value | Language |
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dc.contributor.author | Kim, Yong Man | - |
dc.contributor.author | Jang, Won Hee | - |
dc.contributor.author | Quezado, Martha M | - |
dc.contributor.author | Oh, Yohan | - |
dc.contributor.author | Chung, Kwang Chul | - |
dc.contributor.author | Junn, Eunsung | - |
dc.contributor.author | Mouradian, M. M | - |
dc.date.accessioned | 2022-07-16T19:20:07Z | - |
dc.date.available | 2022-07-16T19:20:07Z | - |
dc.date.created | 2021-05-13 | - |
dc.date.issued | 2011-08 | - |
dc.identifier.issn | 0022-510X | - |
dc.identifier.uri | https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/167751 | - |
dc.description.abstract | Parkinson's disease (PD) and Dementia with Lewy Bodies (DLB) are characterized pathologically by intraneuronal inclusions called Lewy bodies (LBs) and Lewy neurites. A major component of these inclusions is the protein a-synuclein, which is natively unfolded but forms oligomers and insoluble fibrillar aggregates under pathological conditions. Although alpha-synuclein is known to undergo several posttranslational modifications, the contribution of SUMOylation to alpha-synuclein aggregation and the pathogenesis of alpha-synucleinopathies have not been elucidated. Here, we provide evidence that aggregates and inclusions formed as a result of impaired proteasome activity contain SUMOylated alpha-synuclein. Additionally, SUMO1 is present in the halo of LBs colocalizing with alpha-synuclein in the brains of PD and DLB patients. Interestingly. SUMOylation does not affect the ubiquitination of alpha-synuclein. These findings suggest that proteasomal dysfunction results in the accumulation of SUMOylated alpha-synuclein and subsequently its aggregation, pointing to the contribution of this posttranslational modification to the pathogenesis of inclusion formation in alpha-synucleinopathies. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.title | Proteasome inhibition induces alpha-synuclein SUMOylation and aggregate formation | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Oh, Yohan | - |
dc.identifier.doi | 10.1016/j.jns.2011.04.015 | - |
dc.identifier.scopusid | 2-s2.0-79959855550 | - |
dc.identifier.wosid | 000293049500029 | - |
dc.identifier.bibliographicCitation | JOURNAL OF THE NEUROLOGICAL SCIENCES, v.307, no.1-2, pp.157 - 161 | - |
dc.relation.isPartOf | JOURNAL OF THE NEUROLOGICAL SCIENCES | - |
dc.citation.title | JOURNAL OF THE NEUROLOGICAL SCIENCES | - |
dc.citation.volume | 307 | - |
dc.citation.number | 1-2 | - |
dc.citation.startPage | 157 | - |
dc.citation.endPage | 161 | - |
dc.type.rims | ART | - |
dc.type.docType | 정기학술지(Article(Perspective Article포함)) | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Neurosciences & Neurology | - |
dc.relation.journalWebOfScienceCategory | Clinical Neurology | - |
dc.relation.journalWebOfScienceCategory | Neurosciences | - |
dc.subject.keywordPlus | ENHANCED SUMOYLATION | - |
dc.subject.keywordPlus | PARKINSONS-DISEASE | - |
dc.subject.keywordPlus | SUMO MODIFICATION | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | PHOSPHORYLATION | - |
dc.subject.keywordPlus | CONSEQUENCES | - |
dc.subject.keywordPlus | DEGRADATION | - |
dc.subject.keywordPlus | CONJUGATION | - |
dc.subject.keywordPlus | NITRATION | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordAuthor | Parkinson&apos | - |
dc.subject.keywordAuthor | s disease | - |
dc.subject.keywordAuthor | Dementia with Lewy Bodies | - |
dc.subject.keywordAuthor | alpha-Synuclein | - |
dc.subject.keywordAuthor | SUMOylation | - |
dc.subject.keywordAuthor | Protein aggregation | - |
dc.subject.keywordAuthor | Proteasome | - |
dc.identifier.url | https://www.sciencedirect.com/science/article/pii/S0022510X11002188?via%3Dihub | - |
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