葡萄糖诱导的酿酒酵母半乳糖转运蛋白的单泛素化足以发出其内化的信号。
Glucose-induced monoubiquitination of the Saccharomyces cerevisiae galactose transporter is sufficient to signal its internalization.
作者信息
Horak J, Wolf D H
机构信息
Institute of Physiology, Department of Membrane Transport, Academy of Sciences of the Czech Republic, 142 20 Prague, Czech Republic.
出版信息
J Bacteriol. 2001 May;183(10):3083-8. doi: 10.1128/JB.183.10.3083-3088.2001.
Abstract
In Saccharomyces cerevisiae, the addition of glucose to cells growing on galactose induces internalization of the galactose transporter Gal2p and its subsequent proteolysis in the vacuole. Here we report that the essential step in Gal2p down-regulation is its ubiquitination through the Ubc1p-Ubc4p-Ubc5p triad of ubiquitin-conjugating enzymes and Npi1/Rsp5p ubiquitin-protein ligase. Moreover, Gal2p appears to be stabilized in mutant cells defective in the ubiquitin-hydrolase Npi2p/Doa4p, and the mutant phenotype can be reversed by overexpression of ubiquitin. An analysis of the fate of Gal2p in cells overexpressing wild-type ubiquitin as well as its variants incompetent to form polyubiquitin chains showed that monoubiquitination of Gal2p is sufficient to signal internalization of the protein into the endocytic pathway.
摘要
在酿酒酵母中，向以半乳糖为碳源生长的细胞添加葡萄糖会诱导半乳糖转运蛋白Gal2p内化，并随后在液泡中被蛋白酶解。我们在此报告，Gal2p下调的关键步骤是通过泛素结合酶Ubc1p - Ubc4p - Ubc5p三联体和Npi1/Rsp5p泛素 - 蛋白连接酶对其进行泛素化。此外，Gal2p在泛素水解酶Npi2p/Doa4p缺陷的突变细胞中似乎得到稳定，并且突变表型可通过泛素的过表达来逆转。对过表达野生型泛素及其无法形成多聚泛素链的变体的细胞中Gal2p命运的分析表明，Gal2p的单泛素化足以将该蛋白内化信号导入内吞途径。
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