DISTINCT SEQUENCE DETERMINANTS DIRECT INTRACELLULAR SORTING AND MODIFICATION OF A YEAST VACUOLAR PROTEASE
DISTINCT SEQUENCE DETERMINANTS DIRECT INTRACELLULAR SORTING AND MODIFICATION OF A YEAST VACUOLAR PROTEASE
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DOI：
10.1016/0092-8674(87)90084-5
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发表时间：
1987-03-13
期刊：
影响因子：
64.5
通讯作者：
EMR, SD
中科院分区：
文献类型：
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作者：
JOHNSON, LM;BANKAITIS, VA;EMR, SD
我们在液泡糖蛋白羧肽酶 Y (CPY) 中绘制了一个序列决定簇，指导该酶的细胞内分选。通过对由与分泌酶转化酶融合的 CPY 氨基端片段组成的杂合蛋白的研究，我们发现 CPY 的 N 端 50 个氨基酸足以直接将 CPY-Inv 杂合蛋白递送至酵母液泡。我们的数据表明 CPY 的这 50 个氨基酸片段包含两个不同的功能域； N 端信号肽后跟一段包含液泡分选信号的 30 个氨基酸。从野生型 CPY 蛋白中删除这一推定的液泡分选信号会导致 CPY 的错误分选。此外，对 CPY 和 CPY-Inv 杂合蛋白上存在的 Asn 连接寡糖的检查表明，CPY 中的另一个决定因素指定了这些蛋白在高尔基复合体中糖基化的程度。
We have mapped a sequence determinant in the vacuolar glycoprotein carboxypeptidase Y (CPY) that directs intracellular sorting of this enzyme. Through the study of hybrid proteins, consisting of amino-terminal segments of CPY fused to the secretory enzyme invertase, we have found that the N-terminal 50 amino acids of CPY are sufficient to direct delivery of a CPY-Inv hybrid protein to the yeast vacuole. Our data suggest that this 50 amino acid segment of CPY contains two distinct functional domains; an N-terminal signal peptide followed by a segment of 30 amino acids that contains the vacuolar sorting signal. Deletion of this putative vacuole sorting signal from an otherwise wild-type CPY protein leads to missorting of CPY. Furthermore, examination of the Asn-linked oligosaccharides present on CPY and CPY-Inv hybrid proteins suggests that an additional determinant in CPY specifies the extent to which these proteins are glycosylated in the Golgi complex.