Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44
Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44
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DOI：
10.1093/emboj/cdg491
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发表时间：
2003-10-01
期刊：
影响因子：
11.4
通讯作者：
Sitia, R
中科院分区：
文献类型：
--
作者：
Anelli, T;Alessio, M;Sitia, R
二硫键的形成是内质网（ER）分泌蛋白成熟和退出的重要步骤，由特定的ER驻留酶控制。在这个过程中的一个关键因素是Ero 1 alpha，一种缺乏已知ER保留基序的氧化还原蛋白。在这里，我们表明，ERp44介导Ero1 α ER定位通过形成可逆的混合二硫化物。ERp44还阻止具有未配对半胱氨酸的未组装货物蛋白的分泌。我们得出结论，ERp44是巯基介导的保留的关键要素。它也可能有利于二硫键连接的寡聚蛋白质的成熟及其质量控制。
Formation of disulfide bonds, an essential step for the maturation and exit of secretory proteins from the endoplasmic reticulum (ER), is controlled by specific ER-resident enzymes. A pivotal element in this process is Ero1alpha, an oxidoreductin that lacks known ER retention motifs. Here we show that ERp44 mediates Ero1alpha ER localization through the formation of reversible mixed disulfides. ERp44 also prevents the secretion of an unassembled cargo protein with unpaired cysteines. We conclude that ERp44 is a key element in thiol-mediated retention. It might also favour the maturation of disulfide-linked oligomeric proteins and their quality control.