布雷菲尔丁A的作用是通过激活对咳毒素敏感的G蛋白质来阻止的
N T Ktistakis1, M E Linder, M G Roth
1Department of Biochemistry, University of Texas, Southwestern Medical Center, Dallas 75235-9038.
Nature
|March 26, 1992
概括
一种特定的G蛋白调节了外套蛋白如何附着在戈尔吉膜上. 这一发现有助于理解brefeldin A.
科学领域:
- 细胞生物学 细胞生物学
- 分子生物学分子生物学
- 生物化学 生物化学
背景情况:
- 布雷菲尔丁A破坏了哺乳动物细胞中的戈尔吉器官和内质网膜分离.
- 最早观察到的效果是从戈尔吉中释放β-COP外蛋白.
- GTP-gamma S或AlF4-预处理阻断了这种β-COP的释放,表明G蛋白参与其中.
研究的目的:
- 调查异构三基G蛋白在调节毛皮蛋白与戈尔吉膜结合中的作用.
- 为了确定特定的G蛋白子家族是否控制ER和Golgi之间的膜转移.
主要方法:
- 使用了马斯托巴兰,它是异构三基G蛋白的激活剂.
- 在实验室中评估了β-COP与戈尔吉膜的结合.
- 研究了布雷菲尔丁A对穿孔细胞和隔离的戈尔吉膜中的β-COP的影响.
- 研究了咳毒素预治疗对这些相互作用的影响.
主要成果:
- 马斯托帕兰在体外促进了β-COP与戈尔吉膜的结合.
- 马斯托帕兰在细胞和隔离膜系统中对抗了布雷菲尔丁A对β-COP的影响.
- 咳毒素预治疗显著降低了马斯托巴兰对布雷菲尔丁A的抑制作用.
结论:
- 一种异构三体G蛋白,可能来自Gi/Go亚家族,调节了外套蛋白与戈尔吉膜的关联.
- 这种G蛋白在维持戈尔吉-ER分离方面发挥着关键作用.
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