The interaction between calcineurin and α-synuclein is regulated by calcium and calmodulin.
Biochem Biophys Res Commun
; 496(4): 1109-1114, 2018 02 19.
Article
em En
| MEDLINE
| ID: mdl-29409956
ABSTRACT
Calcineurin (CN) is a protein phosphatase and widely distributed in eukaryotes, with an extremely high level of expression in mammalian brain. Alpha-synuclein (α-syn) is a small soluble protein expressed primarily at presynaptic terminals in the central nervous system. In our present study, we explored the interactions between CN and α-syn in vitro. Based on the data from microscale thermophoresis, GST pull-down assays, and co-immunoprecipitation, we found that CN binds α-syn. Furthermore, this interaction is mediated by calcium/calmodulin (Ca2+/CaM) signaling. Additionally, thapsigargin (TG) triggered an increase in CN activity and α-syn aggregation in HEK293â¯cells stably transfected with α-syn. Our previous study in vivo suggest that overexpression of α-syn in transgenic mice significantly promoted CN activity and subsequent nuclear translocation of nuclear factor of activated T-cells (NFAT) in the midbrain dopaminergic (mDA) neurons. These in vivo and in vitro studies have been complementary with each other, representing the changes in the CN-dependent pathway affected by overexpression of α-syn.
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Base de dados:
MEDLINE
Assunto principal:
Calmodulina
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Transdução de Sinais
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Regulação da Expressão Gênica
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Cálcio
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Calcineurina
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Alfa-Sinucleína
Limite:
Humans
Idioma:
En
Revista:
Biochem Biophys Res Commun
Ano de publicação:
2018
Tipo de documento:
Article
País de afiliação:
China