Wang Xuejing, Guo Jifeng, Jiang Hong, Shen Lu, Tang Beisha
Department of Neurology, Xiangya Hospital, Central South University, Changsha 410008, China.
Zhong Nan Da Xue Xue Bao Yi Xue Ban. 2010 Nov;35(11):1156-61. doi: 10.3969/j.issn.1672-7347.2010.11.007.
To explore the interaction between BCL2-associated athanogene 5 (BAG5) and Parkin protein,and the regulatory mechanism of BAG5 protein on the level of Parkin protein.
We performed GST pull-down assay to identify which domain of PINK1 interacted with Parkin, and generated different deletions of BAG5 to identify the domains. Chase time experiment was done to determine the effect of co-regulation of BAG5 protein on the ubiquitination. We further examined the possible interaction between Parkin and PINK1 in 293A cells by co-immunoprecipitation method.
BAG5 directly interacted with the Parkin, and all the 4 BAG domains interacted with the Parkin. BAG5 stabilized the Parkin by interfering its degradation via the ubiquitin-mediated proteasomal pathway.
BAG5 directly interacts with the Parkin, and BAG5 stabilizes the Parkin via the ubiquitin-mediated proteasomal pathway.
探讨BCL2相关抗凋亡基因5(BAG5)与帕金蛋白之间的相互作用,以及BAG5蛋白对帕金蛋白水平的调控机制。
我们进行了谷胱甘肽-S-转移酶下拉试验,以确定PINK1的哪个结构域与帕金相互作用,并对BAG5进行不同的缺失操作以鉴定这些结构域。进行追踪时间实验以确定BAG5蛋白共同调节对泛素化的影响。我们通过免疫共沉淀法进一步检测了293A细胞中帕金与PINK1之间可能的相互作用。
BAG5直接与帕金相互作用,并且所有4个BAG结构域均与帕金相互作用。BAG5通过干扰帕金经泛素介导的蛋白酶体途径的降解来使其稳定。
BAG5直接与帕金相互作用,并且BAG5通过泛素介导的蛋白酶体途径使帕金稳定。