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首页> 外文期刊>Cell biology international. >EXPRESSION OF A CYTOPLASMICALLY EPITOPE-TAGGED HUMAN GOLGI GLYCOSYLTRANSFERASE IN HOMOLOGOUS CELLS RESULTS IN MISLOCALIZATION OF MULTIPLE GOLGI PROTEINS
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EXPRESSION OF A CYTOPLASMICALLY EPITOPE-TAGGED HUMAN GOLGI GLYCOSYLTRANSFERASE IN HOMOLOGOUS CELLS RESULTS IN MISLOCALIZATION OF MULTIPLE GOLGI PROTEINS

机译：细胞膜表位标记的人高尔基糖基糖基转移酶在多种高尔基蛋白错配的同质细胞中的表达

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摘要

We have compared the effect of mislocalization of a Golgi glycosyltransferase in heterologous and homologous cell systems on the distribution of other Golgi-associated proteins. Myc-spacer-human N-acetylglucosaminyltransferase I(NAGT-I), an N-terminally epitope-tagged NAGT-I, in which the first added negatively charged amino acid is in position 13, localizes to the endoplasmic reticulum (ER) by immunofluorescence when expressed in monkey (Vero) or human (HeLa) cells. When myc-spacer-human NAGT-I was expressed in Vero cells, the distribution of the Golgi-associated coat protein, beta-COP, was concentrated juxtanuclearly and undisturbed relative to control. When myc-spacer-human NAGT-I was expressed in HeLa cells, however, both endogenous beta-COP and GalT were no longer concentrated in a juxtanuclear manner but were rather cytoplasmically distributed as was the myc-tagged human NAGT-I. Based on these observations, we suggest that extensive interactions between proteins that normally show overlapping distributions between the medial Golgi stack and trans Golgi/TGN are possible. Moreover, we suggest that small differences in sequence may play a large role in potentiating interactions of Golgi complex proteins. (C) 1997 Academic Press Limited. [References: 26]
机译：我们已经比较了高尔基糖基转移酶在异源和同源细胞系统中的错误定位对其他高尔基体相关蛋白分布的影响。 Myc-spacer-人N-乙酰氨基葡萄糖氨基转移酶I（NAGT-1），是N-末端带有抗原决定基的NAGT-1，其中第一个添加的带负电荷的氨基酸位于13位，通过免疫荧光定位于内质网（ER）当在猴（Vero）或人（HeLa）细胞中表达时。当myc-spacer-human NAGT-1在Vero细胞中表达时，高尔基体相关的外壳蛋白β-COP的分布相对于对照而言，集中并列且不受干扰。但是，当在HeLa细胞中表达myc-spacer-human NAGT-I时，内源性β-COP和GalT都不再以近核方式浓缩，而是像myc标签的人NAGT-I一样在细胞质中分布​​。基于这些观察结果，我们建议通常在内侧高尔基体堆栈与反式高尔基体/ TGN之间显示重叠分布的蛋白质之间的广泛相互作用是可能的。此外，我们建议序列中的细微差异可能在增强高尔基体复杂蛋白的相互作用中发挥重要作用。 （C）1997 Academic Press Limited。 [参考：26]

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