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突触结合蛋白如何促进膜融合。

How synaptotagmin promotes membrane fusion.

作者信息

Martens Sascha, Kozlov Michael M, McMahon Harvey T

机构信息

Medical Research Council-Laboratory of Molecular Biology, Hills Road, CB2 0QH Cambridge, UK.

出版信息

Science. 2007 May 25;316(5828):1205-8. doi: 10.1126/science.1142614. Epub 2007 May 3.

Abstract

Synaptic vesicles loaded with neurotransmitters are exocytosed in a soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE)-dependent manner after presynaptic depolarization induces calcium ion (Ca2+) influx. The Ca2+ sensor required for fast fusion is synaptotagmin-1. The activation energy of bilayer-bilayer fusion is very high (approximately 40 k(B)T). We found that, in response to Ca2+ binding, synaptotagmin-1 could promote SNARE-mediated fusion by lowering this activation barrier by inducing high positive curvature in target membranes on C2-domain membrane insertion. Thus, synaptotagmin-1 triggers the fusion of docked vesicles by local Ca2+-dependent buckling of the plasma membrane together with the zippering of SNAREs. This mechanism may be widely used in membrane fusion.

摘要

在突触前去极化诱导钙离子(Ca2+)内流后,装载神经递质的突触小泡以可溶性N - 乙基马来酰亚胺敏感因子附着蛋白受体(SNARE)依赖的方式进行胞吐作用。快速融合所需的Ca2+传感器是突触结合蛋白-1。双层膜融合的活化能非常高(约40k(B)T)。我们发现,响应Ca2+结合时,突触结合蛋白-1可通过在C2结构域插入膜时诱导靶膜产生高正曲率来降低这一活化能垒,从而促进SNARE介导的融合。因此,突触结合蛋白-1通过质膜局部Ca2+依赖性弯曲以及SNARE的拉链式结合来触发停靠小泡的融合。这种机制可能在膜融合中广泛应用。

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