A HUMAN HOMOLOG OF THE YEAST HDEL RECEPTOR
A HUMAN HOMOLOG OF THE YEAST HDEL RECEPTOR
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DOI：
10.1038/348162a0
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发表时间：
1990-11-08
期刊：
影响因子：
64.8
通讯作者：
PELHAM, HRB
中科院分区：
文献类型：
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作者：
LEWIS, MJ;PELHAM, HRB
酵母和动物细胞通过从卵泡高尔基体或前高尔基体区室中不断回收蛋白质，实现了内质网腔内驻留蛋白质的保留1-3。这些蛋白质的分选依赖于 C 端四肽信号，在动物细胞中通常为 Lys-Asp-Glu-Leu（单字母代码中的 KDEL），在酿酒酵母中通常为 His-Asp-Glu-Leu (HDEL)2,4,5。有证据表明ERD2基因编码识别酵母中HDEL的分选受体6,7；其产品是相对分子质量为 26,000 (26K) 的完整膜蛋白，未糖基化。相反，Vauxet al.8 认为哺乳动物 KDEL 受体是一种 72K 糖蛋白，他们使用抗独特型抗体方法检测到该蛋白。如果真是这样，那就表明酵母和动物细胞之间的修复机制存在惊人的差异。我们在此报道人类细胞表达一种在序列、大小和性质上与ERD2产物相似的蛋白质，并推测该蛋白质是人类KDEL受体。
RETENTION of resident proteins in the lumen of the endoplasmic reticulum is achieved in both yeast and animal cells by their continual retrieval from thecis-Golgi, or a pre-Golgi compartment1–3. Sorting of these proteins is dependent on a C-terminal tetrapeptide signal, usually Lys-Asp-Glu-Leu (KDEL in the single letter code) in animal cells, His-Asp-Glu-Leu (HDEL) inSac-charomyces cerevisiae2,4,5. There is evidence that theERD2gene encodes the sorting receptor that recognizes HDEL in yeast6,7; its product is an integral membrane protein of relative molecular mass 26,000 (26K) that is not glycosylated. In contrast, Vauxet al.8suggest that the mammalian KDEL receptor is a 72K gly-coprotein that they detected using an anti-idiotypic antibody approach. If this were so, it would indicate a surprising divergence of the retrieval machinery between yeast and animal cells. We report here that human cells express a protein similar in sequence, size and properties to theERD2product, and propose that this protein is the human KDEL receptor.