Downregulation of Calnexin expression results in a decrease in Paralytic protein levels, whereas overexpression of the Calnexin C-terminal calcium-binding domain triggers an increase reversely. Co-immunoprecipitation analysis indicates that Calnexin interacts with Paralytic protein variants that contain glycosylation sites Asn313, 325, 343, 1463, and 1482. Here we present evidence that Drosophila ER chaperone Calnexin colocalizes and interacts with the α subunit of sodium channel Paralytic. Chaperone-mediated regulation, one of the major means to control protein quality and function, is an essential route for controlling channel activity. Neuronal activity mediated by voltage-gated channels provides the basis for higher-order behavioral tasks that orchestrate life. 5Key Laboratory of Developmental Genes and Human Disease, Institute of Life Sciences, Southeast University, Nanjing, China.4Shanghai Key Laboratory of Signaling and Diseases Research, School of Life Science and Technology, Institute of Intervention Vessel, Shanghai 10th People's Hospital, Tongji University, Shanghai, China.3Department of Anatomy and Neurobiology, Tongji University School of Medicine, Shanghai, China.2Key Laboratory of Arrhythmias of the Ministry of Education of China, Shanghai East Hospital, Tongji University School of Medicine, Shanghai, China.1Research Center for Translational Medicine, Shanghai East Hospital, Tongji University School of Medicine, Shanghai, China.Xi Xiao 1,2,3†, Changyan Chen 4†, Tian-Ming Yu 1,2,3, Jiayao Ou 1,2,3, Menglong Rui 5, Yuanfen Zhai 1,2,3, Yijing He 1,2,3, Lei Xue 4 and Margaret S.
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