首页> 外文期刊>Journal of Experimental Botany >Arabidopsis SYT1 maintains stability of cortical endoplasmic reticulum networks and VAP27-1-enriched endoplasmic reticulum-plasma membrane contact sites
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Arabidopsis SYT1 maintains stability of cortical endoplasmic reticulum networks and VAP27-1-enriched endoplasmic reticulum-plasma membrane contact sites

机译:拟南芥SYT1维持皮质内质网和富含VAP27-1的内质网-质膜接触部位的稳定性

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摘要

Arabidopsis synaptotagmin 1 is localized on ER-PM contact sites distinct from VAP27-1 and plays roles in maintaining ER morphology and the dynamics of VAP27-1.Arabidopsis synaptotagmin 1 (SYT1) is localized on the endoplasmic reticulum-plasma membrane (ER-PM) contact sites in leaf and root cells. The ER-PM localization of Arabidopsis SYT1 resembles that of the extended synaptotagmins (E-SYTs) in animal cells. In mammals, E-SYTs have been shown to regulate calcium signaling, lipid transfer, and endocytosis. Arabidopsis SYT1 was reported to be essential for maintaining cell integrity and virus movement. This study provides detailed insight into the subcellular localization of SYT1 and VAP27-1, another ER-PM-tethering protein. SYT1 and VAP27-1 were shown to be localized on distinct ER-PM contact sites. The VAP27-1-enriched ER-PM contact sites (V-EPCSs) were always in contact with the SYT1-enriched ER-PM contact sites (S-EPCSs). The V-EPCSs still existed in the leaf epidermal cells of the SYT1 null mutant; however, they were less stable than those in the wild type. The polygonal networks of cortical ER disassembled and the mobility of VAP27-1 protein on the ER-PM contact sites increased in leaf cells of the SYT1 null mutant. These results suggest that SYT1 is responsible for stabilizing the ER network and V-EPCSs.
机译:拟南芥突触标签蛋白1位于与VAP27-1不同的ER-PM接触部位,并在维持ER形态和VAP27-1的动力学中起作用。拟南芥突触标签蛋白1(SYT1)位于内质网-质膜(ER-PM) )叶和根细胞中的接触部位。拟南芥SYT1的ER-PM定位类似于动物细胞中突触突触素(E-SYT)的定位。在哺乳动物中,E-SYTs已显示出调节钙信号传导,脂质转移和内吞作用。据报道,拟南芥SYT1对于维持细胞完整性和病毒运动至关重要。这项研究提供了对SYT1和VAP27-1(另一种ER-PM束缚蛋白)的亚细胞定位的详细了解。 SYT1和VAP27-1已显示位于不同的ER-PM接触部位。富含VAP27-1的ER-PM接触部位(V-EPCS)始终与富含SYT1的ER-PM接触部位(S-EPCS)接触。 V-EPCS仍然存在于SYT1无效突变体的叶表皮细胞中;但是,它们不如野生型稳定。 SYT1 null突变体的叶细胞中,皮质ER的多边形网络分解,ER-PM接触位点上的VAP27-1蛋白迁移率增加。这些结果表明SYT1负责稳定ER网络和V-EPCS。

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