The interaction between calcineurin and ?-synuclein is regulated by calcium and calmodulin.

Calcineurin (CN) is a protein phosphatase and widely distributed in eukaryotes, with an extremely high level of expression in mammalian brain. Alpha-synuclein (?-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 ?-syn ...
in vitro. Based on the data from microscale thermophoresis, GST pull-down assays, and co-immunoprecipitation, we found that CN binds ?-syn. Furthermore, this interaction is mediated by calcium/calmodulin (Ca2+/CaM) signaling. Additionally, thapsigargin (TG) triggered an increase in CN activity and ?-syn aggregation in HEK293?cells stably transfected with ?-syn. Our previous study in vivo suggest that overexpression of ?-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 ?-syn.
Mesh Terms:
Calcineurin, Calcium, Calmodulin, Gene Expression Regulation, HEK293 Cells, Humans, Protein Binding, Protein Interaction Mapping, Signal Transduction, alpha-Synuclein
Biochem. Biophys. Res. Commun.
Date: Dec. 19, 2017
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