突触小泡的v-SNARE蛋白（突触结合蛋白）与质膜的t-SNARE蛋白（SNAP-25）的结合，可以解释在经神经毒素处理的突触处停靠的小泡。
Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses.
作者信息
Schiavo G, Stenbeck G, Rothman J E, Söllner T H
机构信息
Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.
出版信息
Proc Natl Acad Sci U S A. 1997 Feb 4;94(3):997-1001. doi: 10.1073/pnas.94.3.997.
Abstract
Neurotransmitter release requires the specific docking of synaptic vesicles to the presynaptic plasma membrane followed by a calcium-triggered fusion event. Herein we report a previously unsuspected interaction of the synaptic vesicle protein and likely calcium sensor synaptotagmin with the plasma membrane t-SNARE SNAP-25. This interaction appears to resolve the apparent paradox that synaptic vesicles are capable of docking even when VAMP (vesicle-associated membrane protein) or syntaxin is cleaved or deleted and suggests that two species of v-SNAREs (VAMP and synaptotagmin) and two species of t-SNAREs (SNAP-25 and syntaxin) interact to functionally dock synaptic vesicles.
摘要
神经递质的释放需要突触小泡与突触前质膜进行特异性对接，随后发生钙触发的融合事件。在此，我们报告了突触小泡蛋白（可能也是钙传感器）突触结合蛋白与质膜t-SNARE蛋白SNAP-25之间一种此前未被怀疑的相互作用。这种相互作用似乎解决了一个明显的矛盾，即即使VAMP（囊泡相关膜蛋白）或 syntaxin被切割或缺失，突触小泡仍能够对接，这表明两种v-SNARE蛋白（VAMP和突触结合蛋白）和两种t-SNARE蛋白（SNAP-25和syntaxin）相互作用，在功能上使突触小泡对接。
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Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses.突触小泡的v-SNARE蛋白（突触结合蛋白）与质膜的t-SNARE蛋白（SNAP-25）的结合，可以解释在经神经毒素处理的突触处停靠的小泡。
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