SORTING OF SOLUBLE ER PROTEINS IN YEAST
SORTING OF SOLUBLE ER PROTEINS IN YEAST
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DOI：
10.1002/j.1460-2075.1988.tb03005.x
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发表时间：
1988-06-01
期刊：
影响因子：
11.4
通讯作者：
LEWIS, MJ
中科院分区：
文献类型：
--
作者：
PELHAM, HRB;HARDWICK, KG;LEWIS, MJ
在动物细胞中，腔内质网(ER)蛋白被识别C末端序列KDEL的分选系统阻止分泌。我们发现酵母有类似的分选系统，但它识别HDEL，而不是KDEL：承载HDEL信号的酶转化酶的衍生物无法分泌。保留在细胞中的转化酶融合蛋白部分地被驻留在高尔基元件中的外链甘露糖基转移酶修饰。这支持了基于动物细胞研究的观点，即内质网靶向是通过不断从高尔基体中提取蛋白质来实现的。我们已经使用转化酶融合基因来筛选在这个分类系统中有缺陷的突变体。获得了60多个突变；其中8个是单个基因erd1的等位基因。突变株在30℃下生长正常。C，但它们不是将融合蛋白保留在细胞中，而是分泌它。
In animal cells, luminal endoplasmic reticulum (ER) proteins are prevented from being secreted by a sorting system that recognizes the C-terminal sequence KDEL. We show that yeast has a similar sorting system, but it recognizes HDEL, rather than KDEL: derivatives of the enzyme invertase that bear the HDEL signal fail to be secreted. An invertase fusion protein that is retained in the cells is partially modified by outer-chain mannosyl transferase, which reside in the Golgi element. This supports the view, based on studies in animal cells, that ER targeting is achieved by continuous retrieval of proteins from the Golgi. We have used an invertase fusion gene to screen for mutants that are defective in this sorting system. Over 60 mutants were obtained; eight of these are alleles of a single gene, erd1. The mutant strains grow normally at 30.degree. C, but instead of retaining the fusion protein in the cells, they secrete it.