Protein disulfide isomerase A6 promotes the repair of injured nerve through interactions with spastin

基因敲除 细胞生物学 免疫沉淀 微管 化学 神经科学 生物 生物化学 基因
作者
Jian-Xian Luo,Min Xie,Cheng Peng,Yanming Ma,Ke Wang,Gengxiong Lin,Hua Gui Yang,Tianjun Chen,Qiu-Ling Liu,Guowei Zhang,Hong-sheng Lin,Zhisheng Ji
出处
期刊:Frontiers in Molecular Neuroscience [Frontiers Media]
卷期号:15
标识
DOI:10.3389/fnmol.2022.950586
摘要

The maintenance of appropriate endoplasmic reticulum (ER) homeostasis is critical to effective spinal cord injury (SCI) repair. In previous reports, protein disulfide isomerase A6 (PDIA6) demonstrated to serve as a reversible functional modulator of ER stress responses, while spastin can coordinate ER organization through the modulation of the dynamic microtubule network surrounding this organelle. While both PDIA6 and spastin are thus important regulators of the ER, whether they interact with one another for SCI repair still needs to be determined. Here a proteomics analysis identified PDIA6 as being related to SCI repair, and protein interaction mass spectrometry further confirmed the ability of PDIA6 and spastin to interact with one another. Pull-down and co-immunoprecipitation assays were further performed to validate and characterize the interactions between these two proteins. The RNAi-based knockdown of PDIA6 in COS-7 cells inhibited the activity of spastin-dependent microtubule severing. PDIA6 was also found to promote injured neuron repair, while spastin knockdown reversed this reparative activity. Together, these results thus confirm that PDIA6 and spastin function together as critical mediators of nerve repair, highlighting their potential value as validated targets for efforts to promote SCI repair.
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