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- W2074920372 abstract "Mutations in alpha-synuclein, a protein highly enriched in presynaptic terminals, have been implicated in the expression of familial forms of Parkinson's disease (PD) whereas native alpha-synuclein is a major component of intraneuronal inclusion bodies characteristic of PD and other neurodegenerative disorders. Although overexpression of human alpha-synuclein induces dopaminergic nerve terminal degeneration, the molecular mechanism by which alpha-synuclein contributes to the degeneration of these pathways remains enigmatic. We report here that alpha-synuclein complexes with the presynaptic human dopamine transporter (hDAT) in both neurons and cotransfected cells through the direct binding of the non-A beta amyloid component of alpha-synuclein to the carboxyl-terminal tail of the hDAT. alpha-Synuclein--hDAT complex formation facilitates the membrane clustering of the DAT, thereby accelerating cellular dopamine uptake and dopamine-induced cellular apoptosis. Since the selective vulnerability of dopaminergic neurons in PD has been ascribed in part to oxidative stress as a result of the cellular overaccumulation of dopamine or dopamine-like molecules by the presynaptic DAT, these data provide mechanistic insight into the mode by which the activity of these two proteins may give rise to this process." @default.
- W2074920372 created "2016-06-24" @default.
- W2074920372 creator A5005020676 @default.
- W2074920372 creator A5017325982 @default.
- W2074920372 creator A5054347925 @default.
- W2074920372 creator A5085025467 @default.
- W2074920372 date "2001-04-01" @default.
- W2074920372 modified "2023-10-16" @default.
- W2074920372 title "Direct binding and functional coupling of α-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis" @default.
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- W2074920372 doi "https://doi.org/10.1096/fj.00-0334com" @default.
- W2074920372 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11292651" @default.
- W2074920372 hasPublicationYear "2001" @default.
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