Nuclear Localization of α-synuclein and Its Interaction with Histones†
Document Type
Article
Publication Date
2003
Keywords
Aggregation, Fluorescence, Nanofibers, Peptides and Proteins, Rodent Models
Digital Object Identifier (DOI)
https://doi.org/10.1021/bi0341152
Abstract
The aggregation of α-synuclein is believed to play an important role in the pathogenesis of Parkinson's disease as well as other neurodegenerative disorders (“synucleinopathies”). However, the function of α-synuclein under physiologic and pathological conditions is unknown, and the mechanism of α-synuclein aggregation is not well understood. Here we show that α-synuclein forms a tight 2:1 complex with histones and that the fibrillation rate of α-synuclein is dramatically accelerated in the presence of histones in vitro. We also describe the presence of α-synuclein and its co-localization with histones in the nuclei of nigral neurons from mice exposed to a toxic insult (i.e., injections of the herbicide paraquat). These observations indicate that translocation into the nucleus and binding with histones represent potential mechanisms underlying α-synuclein pathophysiology.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Biochemistry, v. 42, p. 8465-8471
Scholar Commons Citation
Goers, John; Manning-Bog, Amy B.; McCormack, Alison L.; Millett, Ian S.; Doniach, Sebastian; Di Monte, Donato A.; Uversky, Vladimir N.; and Fink, Anthony L., "Nuclear Localization of α-synuclein and Its Interaction with Histones†" (2003). Molecular Medicine Faculty Publications. 712.
https://digitalcommons.usf.edu/mme_facpub/712
