The Saccharomyces cerevisiae MBOAT O-acyltransferase Gup1 is involved in many processes, including cell wall and membrane composition and integrity, and acetic acid-induced cell death. Gup1 was previously shown to interact physically with the mitochondrial membrane VDAC (Voltage-Dependent Anion Channel) protein Por1 and the ammonium transceptor Mep2. By co-immunoprecipitation, the eisosome core component Pil1 was identified as a novel physical interaction partner of Gup1. The expression of PIL1 and Pil1 protein levels were found to be unaffected by GUP1 deletion. In ∆gup1 cells, Pil1 was distributed in dots (likely representing eisosomes) in the membrane, identically to wt cells. However, ∆gup1 cells presented 50% less Pil1-GFP dots/eisosomes, suggesting that Gup1 is important for eisosome formation. The two proteins also interact genetically in the maintenance of cell wall integrity, and during arsenite and acetic acid exposure. We show that Δgup1 Δpil1 cells take up more arsenite than wt and are extremely sensitive to arsenite and to acetic acid treatments. The latter causes a severe apoptotic wt-like cell death phenotype, epistatically reverting the ∆gup1 necrotic type of death. Gup1 and Pil1 are thus physically, genetically and functionally connected.

中文翻译：

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eisosome 蛋白 Pil1 和 MBOAT O-酰基转移酶 Gup1 之间的物理、遗传和功能相互作用

的酿酒酵母MBOAT ö -acyltransferase Gup1参与许多过程，包括细胞壁和膜组成和完整性，和乙酸诱导的细胞死亡。Gup1 先前已被证明与线粒体膜 VDAC（电压依赖性阴离子通道）蛋白 Por1 和铵离子转运体 Mep2 发生物理相互作用。通过免疫共沉淀，eisosome 核心成分 Pil1 被确定为 Gup1 的新型物理相互作用伙伴。的表达PIL1和Pil1蛋白水平被认为是由不受影响GUP1删除。在∆gup1细胞中，Pil1 分布在膜中的点（可能代表 eisosomes）中，与wt相同细胞。然而，Δgup1细胞呈现的 Pil1-GFP 点/eisosomes 少 50%，表明 Gup1 对 eisosome 形成很重要。这两种蛋白质还在维持细胞壁完整性方面以及在亚砷酸盐和乙酸暴露期间发生遗传相互作用。我们表明Δgup1 Δpil1细胞比 wt 吸收更多的亚砷酸盐，并且对亚砷酸盐和乙酸处理极为敏感。后者导致严重的凋亡wt样细胞死亡表型，上位性恢复Δgup1坏死类型的死亡。Gup1 和 Pil1 因此在物理上、遗传上和功能上是相连的。