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Essential role for diacylglycerol in protein transport from the yeast Golgi complex

机译:二酰基甘油在酵母高尔基复合体蛋白质转运中的重要作用

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Yeast phosphatidylinositol transfer protein (Sec14p) is required for the production of secretory vesicles from the Golgi. This requirement can be relieved by inactivation of the cytosine 5'-diphosphate (CDP)-choline pathway for phosphatidylcholine biosynthesis, indicating that Sec14p is an essential component of a regulatory pathway linking phospholipid metabolism with vesicle trafficking (the Sec14p pathway). Sac1p (refs 7 and 8) is an integral membrane protein related to inositol-5-phosphatases such as synaptojanin, a protein found in rat brain. Here we show that defects in Sac1p also relieve the requirement for Sec14p by altering phospholipid metabolism so as to expand the pool of diacylglycerol (DAG) in the Golgi. Moreover, although short-chain DAG improves secretory function in strains with a temperature-sensitive Sec14p, expression of diacylglycerol kinase from Escherichia coli further impairs it. The essential function of Sec14p may therefore be to maintain a sufficient pool of DAG in the Golgi to support the production of secretory vesicles.
机译:酵母磷脂酰肌醇转移蛋白(Sec14p)是高尔基生产分泌囊泡所必需的。可以通过灭活磷脂酰胆碱生物合成的胞嘧啶5'-二磷酸(CDP)-胆碱途径来缓解此要求,这表明Sec14p是连接磷脂代谢与囊泡运输(Sec14p途径)的调控途径的重要组成部分。 Sac1p(参考文献7和8)是与肌醇5磷酸酶有关的完整膜蛋白,例如在大鼠脑中发现的突触结合蛋白。在这里,我们表明Sac1p中的缺陷还通过改变磷脂代谢来减轻Sec14p的需求,从而扩大了高尔基体中的二酰基甘油(DAG)库。此外,尽管短链DAG改善了对温度敏感的Sec14p菌株的分泌功能,但大肠杆菌中的二酰基甘油激酶的表达进一步损害了它。因此,Sec14p的基本功能可能是在高尔基体中维持足够的DAG库,以支持分泌性小泡的产生。

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