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首页> 外文期刊>The FEBS journal >Specific membrane binding of the carboxypeptidase Y inhibitor I-C, a phosphatidylethanolamine-binding protein family member
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Specific membrane binding of the carboxypeptidase Y inhibitor I-C, a phosphatidylethanolamine-binding protein family member

机译：羧肽酶Y抑制剂I-C（磷脂酰乙醇胺结合蛋白家族成员）的特异性膜结合

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摘要

I-C, an endogenous cytoplasmic inhibitor of vacuolar carboxypeptidase Y in the yeast Saccharomyces cerevisiae, is classified as a member of the phosphatidylethanolamine-binding protein family. The binding of I-C to phospholipid membranes was first analyzed using a liposome-binding assay and by surface plasmon resonance measurements, which revealed that the affinity of this inhibitor was not for phosphatidylethanolamine but for anionic phospholipids, such as phosphatidylserine, phosphatidylinositol 3-phosphate, phosphatidylinositol 3,4-bisphosphate, and phosphatidylinositol 3,4,5-trisphosphate, with K-D values below 100 nM. The liposome-binding assay and surface plasmon resonance analyses of I-C, when complexed with carboxypeptidase Y, and the mutant forms of I-C further suggest that the N-terminal segment (Met1-His18) in its carboxypeptidase Y-binding sites is involved in the specific and efficient binding to anionic phospholipid membranes. The binding of I-C to cellular membranes was subsequently analyzed by fluorescence microscopy of yeast cells producing the green fluorescent protein-tagged I-C, suggesting that I-C is specifically targeted to vacuolar membranes rather than cytoplasmic membranes, during the stationary growth phase. The present findings provide novel insights into the membrane-targeting and biological functions of I-C and phosphatidylethanolamine-binding proteins.
机译：I-C是酿酒酵母（Saccharomyces cerevisiae）中液泡羧肽酶Y的内源性细胞质抑制剂，被归类为磷脂酰乙醇胺结合蛋白家族的成员。首先使用脂质体结合测定法和通过表面等离子体共振测量来分析IC与磷脂膜的结合，这表明该抑制剂的亲和力不是对磷脂酰乙醇胺而是对阴离子磷脂，如磷脂酰丝氨酸，磷脂酰肌醇3-磷酸酯，磷脂酰肌醇3,4-双磷酸酯和磷脂酰肌醇3,4,5-三磷酸酯，KD值低于100 nM。当与羧肽酶Y复合时，IC的脂质体结合测定和表面等离振子共振分析以及IC的突变形式进一步表明，其羧肽酶Y结合位点的N末端片段（Met1-His18）参与了特异性与阴离子磷脂膜的有效结合。随后，通过产生绿色荧光蛋白标签的I-C的酵母细胞的荧光显微镜检查，对I-C与细胞膜的结合进行了分析，表明I-C在固定生长期专门针对液泡膜而不是细胞质膜。本发现为I-C和磷脂酰乙醇胺结合蛋白的膜靶向和生物学功能提供了新颖的见解。

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