Analysis of synphilin-1 and synuclein interactions by yeast two-hybrid beta-galactosidase liquid assay.
Neurosci Lett
; 325(2): 119-23, 2002 Jun 07.
Article
em En
| MEDLINE
| ID: mdl-12044636
ABSTRACT
Synphilin-1 interacts with alpha-synuclein, which has been implicated in the pathogenesis of Parkinson's disease (PD). By examination of their interactions quantitatively, with the use of the yeast two-hybrid beta-galactosidase assay, we find that the synuclein amino acid (aa) 1-65 region is sufficient for an interaction. A central domain of synphilin-1, aa 349-555, is both necessary and sufficient for an interaction with alpha-synuclein. We did not observe an effect of the synuclein A53T mutation, which causes one familial form of PD, on interactions with synphilin-1. However, the A30P mutation caused an increase in the interaction between the synuclein aa 1-65 fragment and the synphilin-1 central domain.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas de Transporte
/
Proteínas do Tecido Nervoso
Limite:
Humans
Idioma:
En
Revista:
Neurosci Lett
Ano de publicação:
2002
Tipo de documento:
Article
País de afiliação:
Estados Unidos