期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 496, 期 4, 页码 1109-1114出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2018.01.148
关键词
Alpha-synuclein; Calcineurin; Microscale thermophoresis; GST pull-down assays; Co-immunoprecipitation; Thapsigargin
资金
- National Nature Science Foundation of China [81373389, 31540011]
Calcineurin (CN) is a protein phosphatase and widely distributed in eukaryotes, with an extremely high level of expression in mammalian brain. Alpha-synuclein (alpha-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 alpha-syn in vitro. Based on the data from microscale thermophoresis, GST pull down assays, and co-immunoprecipitation, we found that CN binds alpha-syn. Furthermore, this interaction is mediated by calciumicalmodulin (Ca2+/CaM) signaling. Additionally, thapsigargin (TG) triggered an increase in CN activity and alpha-syn aggregation in HEK293 cells stably transfected with alpha-syn. Our previous study in vivo suggest that overexpression of alpha-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 alpha-syn. (C) 2018 Elsevier Inc. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据