THE SORTING RECEPTOR FOR YEAST VACUOLAR CARBOXYPEPTIDASE-Y IS ENCODED BY THE VPS10 GENE
THE SORTING RECEPTOR FOR YEAST VACUOLAR CARBOXYPEPTIDASE-Y IS ENCODED BY THE VPS10 GENE
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DOI：
10.1016/0092-8674(94)90219-4
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发表时间：
1994-05-20
期刊：
影响因子：
64.5
通讯作者：
EMR, SD
中科院分区：
文献类型：
--
作者：
MARCUSSON, EG;HORAZDOVSKY, BF;EMR, SD
酿酒酵母液泡蛋白分选（VPS10）基因编码可溶性液泡蛋白羧肽酶Y （CPY）分选所需的1577个氨基酸的I型跨膜蛋白。VPS10的突变导致CPY的选择性错选和分泌；在vps10突变体中，所有其他测试的液泡蛋白都被传递到液泡中。化学交联研究表明，Vps10p与高尔基修饰的CPY前体形式直接相互作用。CPY液泡分选信号中单个氨基酸的改变阻止了这种相互作用。Vps10p还与含有CPY分选信号的杂交蛋白相互作用，该杂交蛋白与正常分泌的酶转化酶融合。亚细胞分离表明，大部分Vps10p定位于高尔基隔室，在那里液泡蛋白被分选。我们提出VPS10编码CPY分选受体，该受体通过在晚期高尔基体和泡前核内体样隔室之间循环进行多轮分选。
The S. cerevisiae VPS10 (vacuolar protein sorting) gene encodes a type I transmembrane protein of 1577 amino acids required for the sorting of the soluble vacuolar protein carboxypeptidase Y (CPY). Mutations in VPS10 result in the selective missorting and secretion of CPY; all other vacuolar proteins tested are delivered to the vacuole in vps10 mutants. Chemical cross-linking studies demonstrate that Vps10p and the Golgi-modified precursor form of CPY directly interact. A single amino acid change in the CPY vacuolar sorting signal prevents this interaction. Vps10p also interacts with a hybrid protein containing the CPY sorting signal fused to the normally secreted enzyme invertase. Subcellular fractionation indicates that the majority of Vps10p is localized to a late Golgi compartment where vacuolar proteins are sorted. We propose that VPS10 encodes a CPY sorting receptor that executes multiple rounds of sorting by cycling between the late Golgi and a prevacuolar endosome-like compartment.