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首页> 外文期刊>Neuron >SNARE protein recycling by alphaSNAP and betaSNAP supports synaptic vesicle priming.
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SNARE protein recycling by alphaSNAP and betaSNAP supports synaptic vesicle priming.

机译：通过alphaSNAP和betaSNAP进行的SNARE蛋白回收支持突触小泡引发。

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摘要

Neurotransmitter release proceeds by Ca(2+)-triggered, SNARE-complex-dependent synaptic vesicle fusion. After fusion, the ATPase NSF and its cofactors alpha- and betaSNAP disassemble SNARE complexes, thereby recycling individual SNAREs for subsequent fusion reactions. We examined the effects of genetic perturbation of alpha- and betaSNAP expression on synaptic vesicle exocytosis, employing a new Ca(2+) uncaging protocol to study synaptic vesicle trafficking, priming, and fusion in small glutamatergic synapses of hippocampal neurons. By characterizing this protocol, we show that synchronous and asynchronous transmitter release involve different Ca(2+) sensors and are not caused by distinct releasable vesicle pools, and that tonic transmitter release is due to ongoing priming and fusion of new synaptic vesicles during high synaptic activity. Our analysis of alpha- and betaSNAP deletion mutant neurons shows that the two NSF cofactors support synaptic vesicle priming by determining the availability of free SNARE components, particularly during phases of high synaptic activity.
机译：由Ca（2+）触发，SNARE复杂依赖突触囊泡融合进行神经递质释放。融合后，ATPase NSF及其辅因子α-和betaSNAP分解SNARE复合物，从而回收单个SNARE，以进行后续的融合反应。我们检查了α-和βSNAP表达对突触囊泡胞吐作用的遗传扰动的影响，采用新的Ca（2+）解笼协议来研究突触囊泡的运输，启动和海马神经元小谷氨酸能突触的融合。通过表征此协议，我们表明同步和异步发射器释放涉及不同的Ca（2+）传感器，并且不是由不同的可释放囊泡池引起的，并且进补发射器的释放是由于新的突触囊泡在高突触过程中持续引发和融合而引起的活动。我们对alpha和betaSNAP缺失突变神经元的分析表明，这两个NSF辅助因子通过确定游离SNARE组分的可用性来支持突触小泡引发，特别是在高突触活性阶段。

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