Imaging Sphingomyelin- and Cholesterol-Enriched Domains in the Plasma Membrane Using a Novel Probe and Super-Resolution Microscopy
Imaging Sphingomyelin- and Cholesterol-Enriched Domains in the Plasma Membrane Using a Novel Probe and Super-Resolution Microscopy
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使用新型探针和超分辨率显微镜对质膜中富含鞘磷脂和胆固醇的结构域进行成像
DOI：
10.1007/978-981-33-6064-8_4
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发表时间：
2021
期刊：
影响因子：
--
通讯作者：
Kobayashi Toshihide
中科院分区：
文献类型：
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作者：
Abe Mitsuhiro;Kobayashi Toshihide
在本章中，我们展示了使用特定的脂质结合蛋白和超分辨率显微镜的脂质结构域的可视化。脂筏是富含鞘脂和甾醇的质膜结构域，在各种生理事件中起关键作用。我们鉴定了一种新的蛋白质，其特异性结合鞘磷脂（SM）和胆固醇（Chol）的复合物。分离的蛋白质nakanori标记哺乳动物细胞质膜外小叶处的SM/Chol复合物。结构化照明显微图像表明，流感病毒从MDCK细胞中SM/Chol结构域的边缘出芽。此外，光活化定位显微镜分析表明，SM/胆固醇复合物的形式域的外叶，磷脂酰肌醇4，5-二磷酸结构域的内叶。这些观察为深入了解脂筏的结构和功能提供了重要信息。
In this chapter, we show the visualization of lipid domains using a specific lipid-binding protein and super-resolution microscopy. Lipid rafts are plasma membrane domains enriched in both sphingolipids and sterols that play key roles in various physiological events. We identified a novel protein that specifically binds to a complex of sphingomyelin (SM) and cholesterol (Chol). The isolated protein, nakanori, labels the SM/Chol complex at the outer leaflet of the plasma membrane in mammalian cells. Structured illumination microscopic images suggested that the influenza virus buds from the edges of the SM/Chol domains in MDCK cells. Furthermore, a photoactivated localization microscopy analysis indicated that the SM/Chol complex forms domains in the outer leaflet, just above the phosphatidylinositol 4,5-bisphosphate domains in the inner leaflet. These observations provide significant insight into the structure and function of lipid rafts.