α-Synuclein is phosphorylated in synucleinopathy lesions View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-02

AUTHORS

Hideo Fujiwara, Masato Hasegawa, Naoshi Dohmae, Akiko Kawashima, Eliezer Masliah, Matthew S Goldberg, Jie Shen, Koji Takio, Takeshi Iwatsubo

ABSTRACT

The deposition of the abundant presynaptic brain protein alpha-synuclein as fibrillary aggregates in neurons or glial cells is a hallmark lesion in a subset of neurodegenerative disorders. These disorders include Parkinson's disease (PD), dementia with Lewy bodies (DLB) and multiple system atrophy, collectively referred to as synucleinopathies. Importantly, the identification of missense mutations in the alpha-synuclein gene in some pedigrees of familial PD has strongly implicated alpha-synuclein in the pathogenesis of PD and other synucleinopathies. However, specific post-translational modifications that underlie the aggregation of alpha-synuclein in affected brains have not, as yet, been identified. Here, we show by mass spectrometry analysis and studies with an antibody that specifically recognizes phospho-Ser 129 of alpha-synuclein, that this residue is selectively and extensively phosphorylated in synucleinopathy lesions. Furthermore, phosphorylation of alpha-synuclein at Ser 129 promoted fibril formation in vitro. These results highlight the importance of phosphorylation of filamentous proteins in the pathogenesis of neurodegenerative disorders. More... »

PAGES

160-164

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncb748

DOI

http://dx.doi.org/10.1038/ncb748

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1010944863

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11813001


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