Semisynthetic, site-specific ubiquitin modification of α-synuclein reveals differential effects on aggregation.
J Am Chem Soc
; 134(12): 5468-71, 2012 Mar 28.
Article
em En
| MEDLINE
| ID: mdl-22404520
ABSTRACT
The process of neurodegeneration in Parkinson's Disease is intimately associated with the aggregation of the protein α-synuclein into toxic oligomers and fibrils. Interestingly, many of these protein aggregates are found to be post-translationally modified by ubiquitin at several different lysine residues. However, the inability to generate homogeneously ubiquitin modified α-synuclein at each site has prevented the understanding of the specific biochemical consequences. We have used protein semisynthesis to generate nine site-specifically ubiquitin modified α-synuclein derivatives and have demonstrated that different ubiquitination sites have differential effects on α-synuclein aggregation.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Ubiquitina
/
Alfa-Sinucleína
Tipo de estudo:
Prognostic_studies
Limite:
Humans
Idioma:
En
Ano de publicação:
2012
Tipo de documento:
Article