Glucose-Induced Monoubiquitination of the Saccharomyces cerevisiae Galactose Transporter Is Sufficient To Signal Its Internalization

Jaroslav Horak; Dieter H. Wolf

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Glucose-Induced Monoubiquitination of the Saccharomyces cerevisiae Galactose Transporter Is Sufficient To Signal Its Internalization

机译：酿酒酵母半乳糖转运蛋白的葡萄糖诱导的单泛素化足以表明其内在化。

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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.

机译：在中，向半乳糖上生长的细胞添加葡萄糖会诱导半乳糖转运蛋白Gal2p的内在化，并随后在液泡中进行蛋白水解。在这里，我们报道Gal2p下调的关键步骤是通过Ubc1p-Ubc4p-Ubc5p三联体的泛素结合酶和Npi1 / Rsp5p泛素蛋白连接酶使其泛素化。此外，Gal2p似乎在泛素水解酶Npi2p / Doa4p缺陷的突变细胞中稳定，并且突变体表型可以通过泛素的过表达来逆转。对Gal2p在过表达野生型遍在蛋白及其不能形成聚遍在蛋白链的变体中的命运的分析表明，Gal2p的单遍在蛋白化足以表明该蛋白内在化进入内吞途径。

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《Journal of bacteriology》 |2001年第10期|共6页
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Jaroslav Horak; Dieter H. Wolf;
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1. Monoubiquitination Is Sufficient To Signal Internalization of the Maltose Transporter in Saccharomyces cerevisiae [J] . Pilar Lucero, élida Pe?alver, Laura Vela, Journal of bacteriology . 2000,第1期

机译：单泛素化足以表明啤酒酵母中麦芽糖转运蛋白的内在化。
2. Sequences in the N-terminal cytoplasmic domain of Saccharomyces cerevisiae maltose permease are required for vacuolar degradation but not glucose-induced internalization. [J] . Gadura N, Michels CA Current Genetics: Eukaryotes with Emphasis on Yeasts, Fungi, Mitochondria, Plastids . 2006,第2期

机译：酿酒酵母麦芽糖通透酶的N-末端胞质结构域中的序列是液泡降解所需的，而不是葡萄糖诱导的内在化。
3. Sequences in the N-terminal cytoplasmic domain of Saccharomyces cerevisiae maltose permease are required for vacuolar degradation but not glucose-induced internalization [J] . Nidhi Gadura, Corinne A. Michels Current Genetics . 2006,第2期

机译：液泡降解需要酿酒酵母麦芽糖通透酶N端细胞质结构域的序列，而不是葡萄糖诱导的内在化
4. Increasing Galactose Utilized Ability of Saccharomyces cerevisiae Through Gene Engineering [C] . Tong Shen, Xuewu Guo, Jing Zou, International conference on applied biotechnology . 2014

机译：通过基因工程提高酿酒酵母的半乳糖利用能力
5. Identification and characterization of two glucose sensing/signaling pathways stimulating glucose-induced inactivation of maltose permease in Saccharomyces. [D] . Jiang, Hua. 1997

机译：鉴定和表征刺激葡萄糖诱导的酵母菌中的麦芽糖通透酶失活的两个葡萄糖传感/信号通路。
6. Glucose-Induced Monoubiquitination of the Saccharomyces cerevisiae Galactose Transporter Is Sufficient To Signal Its Internalization [O] . Jaroslav Horak, Dieter H. Wolf 2001

机译：酿酒酵母半乳糖转运蛋白的葡萄糖诱导的单泛素化足以表明其内在化。
7. Glucose-Induced Monoubiquitination of the Saccharomyces cerevisiae Galactose Transporter Is Sufficient To Signal Its Internalization [O] . Horak, Jaroslav, Wolf, Dieter H. 2001

机译：酿酒酵母半乳糖转运蛋白的葡萄糖诱导的单泛素化足以表明其内在化。

Glucose-Induced Monoubiquitination of the Saccharomyces cerevisiae Galactose Transporter Is Sufficient To Signal Its Internalization

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