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机构地区:[1]华中科技大学生命科学与技术学院生物物理与生物化学所,武汉市430077
出 处:《医学分子生物学杂志》2004年第2期110-112,共3页Journal of Medical Molecular Biology
基 金:国家自然科学基金(30025023;3000062;30130230);国家高技术发展规划项目(973) (G1999054000;2001CCA04100)
摘 要:Secl/Munc-18(SM)蛋白是一类与分泌相关的亲水性蛋白质,能以多种结合方式与可溶性N-乙基马莱酰胺敏感因子(NSF)附着蛋白受体(SNARE)的Syntaxin蛋白家族结合,进而参与细胞的分泌调控。虽然SM蛋白对于细胞分泌至关重要,但是SM蛋白调节细胞分泌的分子机制尚不清楚。SM蛋白可能主要在囊泡的锚定(docking)过程中起作用,但是也有文献表明SM蛋白可能也参与锚定以后的启动(priming)、融合(fusion)等分泌步骤中的调控。Sec1/Munc-18 (SM) proteins are hydrophilic proteins associated with exocytosis. Deletion of SM proteins abolishes the respective fusion event, demonstrating that SM proteins are essential for vesicle transportation and intracellular membrane fusion reactions. Most of SM proteins bind to membrane-associated soluble N-ethylmaleimide-sensitive fusion attachment protein receptors (SNAREs) of the Syntaxin subfamily but the mechanism of Syntaxin binding is unclear. Until now the molecular mechanism of the function of SM proteins is still unknown. Recently, researches showed that the role of SM proteins might be related to the docking of vesicles, and other researches showed that SM proteins might work in a variety of reactions after docking, such as priming and fusion.
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