翻转酶在内质网蛋白糖基化中的作用

Lipid insights Pub Date : 2016-02-21 DOI:10.4137/LPI.S31784
J. Rush
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引用次数: 8

摘要

在真核生物中,糖基化对糖蛋白的合成、折叠和功能至关重要。蛋白质在内质网(ER)中被多种聚糖共同修饰和翻译后修饰;修饰包括C-和o -甘露糖基化,n -糖基化,以及添加糖基磷脂酰肌醇膜锚点。真核生物内质网中的蛋白质糖基化涉及内质网膜细胞质和管腔表面的酶促步骤。聚糖首先作为前体糖脂在内质网的细胞质表面组装,通过附着于含有还原α-异戊二烯的长链聚异戊二烯磷酸(多醇)与膜相连。脂质锚定的构建块然后横向迁移(翻转)穿过内质网膜到管腔表面,在那里完成聚糖的最终组装。这种策略允许细胞输出高能生物合成中间体作为脂质结合聚糖,同时将糖基供体限制在膜表面的组装位点。本文就内质网中参与蛋白糖基化的翻转酶作一综述。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Role of Flippases in Protein Glycosylation in the Endoplasmic Reticulum
Glycosylation is essential to the synthesis, folding, and function of glycoproteins in eukaryotes. Proteins are co- and posttranslationally modified by a variety of glycans in the endoplasmic reticulum (ER); modifications include C- and O-mannosylation, N-glycosylation, and the addition of glycosylphosphatidylinositol membrane anchors. Protein glycosylation in the ER of eukaryotes involves enzymatic steps on both the cytosolic and lumenal surfaces of the ER membrane. The glycans are first assembled as precursor glycolipids, on the cytosolic surface of the ER, which are tethered to the membrane by attachment to a long-chain polyisoprenyl phosphate (dolichol) containing a reduced α-isoprene. The lipid-anchored building blocks then migrate transversely (flip) across the ER membrane to the lumenal surface, where final assembly of the glycan is completed. This strategy allows the cell to export high-energy biosynthetic intermediates as lipid-bound glycans, while constraining the glycosyl donors to the site of assembly on the membrane surface. This review focuses on the flippases that participate in protein glycosylation in the ER.
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