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GRASP65 controls the cis Golgi integrity in vivo

机译：GRASP65在体内控制顺式高尔基体的完整性

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GRASP65 and GRASP55 are peripheral Golgi proteins localized to cis and medial/trans cisternae, respectively. They are implicated in diverse aspects of protein transport and structure related to the Golgi complex, including the stacking of the Golgi stack and/or the linking of mammalian Golgi stacks into the Golgi ribbon. Using a mouse model, we interfered with GRASP65 by homologous recombination and confirmed its absence of expression. Surprisingly, the mice were healthy and fertile with no apparent defects in tissue, cellular or subcellular organization. Immortalized MEFs derived from the mice did not show any growth or morphological defects. However, despite the normal appearance of the Golgi ribbon, a fluorescence recovery after photobleaching assay revealed functional discontinuities specific to the cis cisternal membrane network. This leads to a strong change in the plasma membrane GSII lectin staining that was also observed in certain mutant tissues. These findings substantiate the role of GRASP65 in continuity of the cis Golgi network required for proper glycosylation, while showing that neither this continuity nor GRASP65 itself are essential for the viability of a complex organism.
机译：GRASP65和GRASP55是分别定位于顺式和反式/反式水箱的外周高尔基体蛋白。它们涉及与高尔基体有关的蛋白质运输和结构的各个方面，包括高尔基体的堆叠和/或哺乳动物高尔基体堆叠到高尔基带中。使用小鼠模型，我们通过同源重组干扰了GRASP65，并证实其不存在表达。出人意料的是，这些小鼠既健康又肥沃，在组织，细胞或亚细胞组织中没有明显的缺陷。源自小鼠的永生化MEF没有显示任何生长或形态缺陷。然而，尽管高尔基体带的外观正常，但光漂白测定后的荧光恢复显示了对顺式胸膜网络特异的功能中断。这导致质膜GSII凝集素染色的强烈变化，这在某些突变组织中也观察到。这些发现证实了GRASP65在适当糖基化所需的顺式高尔基体网络的连续性中的作用，同时表明这种连续性或GRASP65本身对于复杂生物的生存力都不是必需的。

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