Nucleotide sugars, nucleotide sulfate, and ATP transporters of the endoplasmic reticulum and Golgi apparatus
Nucleotide sugars, nucleotide sulfate, and ATP transporters of the endoplasmic reticulum and Golgi apparatus
复制标题
DOI：
10.1111/j.1749-6632.1998.tb09636.x
复制
发表时间：
1998-01-01
期刊：
影响因子：
--
通讯作者：
Hirschberg, CB
中科院分区：
文献类型：
--
作者：
Berninsone, P;Hirschberg, CB
内质网和高尔基体的腔是分泌和膜结合蛋白、蛋白聚糖和脂质发生糖基化、硫酸化和磷酸化的亚细胞位点。核苷酸糖、核苷酸硫酸盐和ATP是上述反应中的底物，必须首先从细胞质转移到这些细胞器的内腔中。这些核苷酸衍生物的转运是由高度特异性的转运蛋白介导的，这些转运蛋白是具有相应核苷单磷酸的反向转运蛋白，如哺乳动物和酵母中的遗传和生物化学方法所示。对哺乳动物、酵母和原生动物突变体的研究表明，特定转运蛋白的缺陷会导致体内蛋白质、脂质和蛋白聚糖糖基化的选择性损伤。这些转运蛋白已被纯化，克隆，并发现编码非常疏水的蛋白质与多跨膜结构域。酵母和哺乳动物细胞的实验表明，这些转运蛋白在翻译后修饰中起着调节作用。
The lumina of the endoplasmic reticulum and Golgi apparatus are the subcellular sites where glycosylation, sulfation, and phosphorylation of secretory and membrane-bound proteins, proteoglycans, and lipids occur. Nucleotide sugars, nucleotide sulfate, and ATP are substrates in the above reactions and must first be translocated from the cytosol into the lumen of these organelles. Translocation of these nucleotide derivatives is mediated by highly specific transporters, which are antiporters with the corresponding nucleoside monophosphate, as shown by genetic and biochemical approaches in mammals and yeast. Studies with mammalian, yeast, and protozoa mutants have shown that a defect in a specific translocator results in selective impairments of glycosylation of proteins, lipids and proteoglycans in vivo. Several of these transporters have been purified, cloned, and found to encode very hydrophobic proteins with multitransmembrane domains. Experiments with yeast and mammalian cells demonstrate that these transporters play a regulatory role in posttranslational modifications.