PLK2 modulates α-synuclein aggregation in yeast and mammalian cells.
Mol Neurobiol
; 48(3): 854-62, 2013 Dec.
Article
en En
| MEDLINE
| ID: mdl-23677647
ABSTRACT
Phosphorylation of α-synuclein (aSyn) on serine 129 is one of the major post-translation modifications found in Lewy bodies, the typical pathological hallmark of Parkinson's disease. Here, we found that both PLK2 and PLK3 phosphorylate aSyn on serine 129 in yeast. However, only PLK2 increased aSyn cytotoxicity and the percentage of cells presenting cytoplasmic foci. Consistently, in mammalian cells, PLK2 induced aSyn phosphorylation on serine 129 and induced an increase in the size of the inclusions. Our study supports a role for PLK2 in the generation of aSyn inclusions by a mechanism that does not depend directly on serine 129 phosphorylation.
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Saccharomyces cerevisiae
/
Proteínas Serina-Treonina Quinasas
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Alfa-Sinucleína
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Mol Neurobiol
Asunto de la revista:
BIOLOGIA MOLECULAR
/
NEUROLOGIA
Año:
2013
Tipo del documento:
Article
País de afiliación:
Portugal