Universität des Saarlandes, Institut für Physiologie, Kirrberger Str. 8, D-66421 Homburg/Saar, Germany.
Cell Calcium. 2013 Aug;54(2):105-10. doi: 10.1016/j.ceca.2013.05.003. Epub 2013 May 30.
Snapin associates with SNAP-25 and with assembled SNARE complexes, stabilizing the coupling between Synaptotagmin-1 and SNAP-25. Deletion of Snapin reduces releasable pools of vesicles in chromaffin cells and reduces synchronous release of neurotransmitter in cortical neurons. Snapin deletion leads to a deficit in exocytosis at low calcium concentration with no change in the threshold calcium concentration for exocytosis in chromaffin cells. In order to determine whether Snapin deletion alters release rates or calcium dependence, we examined the effect of overexpression of wild type Snapin on readily releasable pool kinetics and pool size in mouse chromaffin cells. Modest increases in intracellular calcium induced by flash-photolysis unmasked a rapidly releasing component of secretion which was enhanced when Snapin was overexpressed. This result indicates that Snapin allows rapid release at lower intracellular calcium levels at which release of the remaining RRP occurs more slowly.
衔接蛋白与 SNAP-25 和组装的 SNARE 复合物结合,稳定突触融合蛋白 1 和 SNAP-25 之间的偶联。衔接蛋白的缺失减少了嗜铬细胞中可释放的囊泡库,并减少了皮质神经元中神经递质的同步释放。衔接蛋白缺失导致低钙浓度下胞吐作用的缺陷,而嗜铬细胞中胞吐作用的阈钙浓度没有变化。为了确定衔接蛋白缺失是否改变了释放速率或钙依赖性,我们研究了野生型衔接蛋白过表达对小鼠嗜铬细胞中易释放池动力学和池大小的影响。闪光光解诱导的细胞内钙离子适度增加揭示了分泌的快速释放成分,当衔接蛋白过表达时,这种成分得到增强。这一结果表明,衔接蛋白允许在较低的细胞内钙离子水平下进行快速释放,而在这些水平下,剩余的 RRP 的释放速度较慢。