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首页> 外文期刊>Molecular biology of the cell >The transmembrane domain of acid trehalase mediates ubiquitin-independent multivesicular body pathway sorting
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The transmembrane domain of acid trehalase mediates ubiquitin-independent multivesicular body pathway sorting

机译：酸性海藻糖酶的跨膜结构域介导遍在蛋白无胞素的多猪体途径分选

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摘要

Trehalose serves as a storage source of carbon and plays important roles under various stress conditions. For example, in many organisms trehalose has a critical function in preserving membrane structure and fluidity during dehydration/rehydration. In the yeast Saccharomyces cerevisiae, trehalose accumulates in the cell when the nutrient supply is limited but is rapidly degraded when the supply of nutrients is renewed. Hydrolysis of trehalose in yeast depends on neutral trehalase and acid trehalase (Ath1). Ath1 resides and functions in the vacuole; however, it appears to catalyze the hydrolysis of extracellular trehalose. Little is known about the transport route of Ath1 to the vacuole or how it encounters its substrate. Here, through the use of various trafficking mutants we showed that this hydrolase reaches its final destination through the multivesicular body (MVB) pathway. In contrast to the vast majority of proteins sorted into this pathway, Ath1 does not require ubiquitination for proper localization. Mutagenesis analyses aimed at identifying the unknown targeting signal revealed that the transmembrane domain of Ath1 contains the information sufficient for its selective sequestration into MVB internal vesicles.
机译：海藻糖用作碳的储存来源，并在各种压力条件下发挥重要作用。例如，在许多生物体中，海藻糖具有在脱水/再水合过程中保持膜结构和流动性的关键作用。在酵母酿酒酵母中，当营养供应有限时，海藻糖在细胞中积聚在细胞中，但在更新营养素供应时迅速降解。酵母中海藻糖的水解取决于中性海藻糖酶和酸性海藻酶（ATH1）。 Ath1在液泡中居住和功能;然而，它似乎催化了细胞外海藻糖的水解。关于Ath1的运输路线对液泡或其如何遇到其基质的情况知之甚少。这里，通过使用各种贩运突变体，我们表明该水解酶通过多猪体（MVB）途径达到其最终目的地。与大多数蛋白质相比，分类为该途径，Ath1不需要泛素化以进行适当的定位。旨在识别未知靶向信号的诱变分析显示ATH1的跨膜结构域包含足以其选择性地螯合成MVB内部囊泡的信息。

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