Söllner Thomas H
Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, Box 519, New York, NY 10021, USA.
Mol Membr Biol. 2003 Jul-Sep;20(3):209-20. doi: 10.1080/0968768031000104953.
The pairing of cognate v- and t-SNAREs between two opposing lipid bilayers drives spontaneous membrane fusion and confers specificity to intracellular membrane trafficking. These fusion events are regulated by a cascade of protein-protein interactions that locally control SNARE activity and complex assembly, determining when and where fusion occurs with high efficiency in vivo. This basic regulation occurs at all transport steps and is mediated by conserved protein families such as Rab proteins and their effectors and Sec1/unc18 proteins. Regulated exocytosis employs auxiliary components that couple the signal (which triggers exocytosis) to the fusion machinery. At the neuronal synapse, munc13 as well as munc18 control SNARE complex assembly. Synaptotagmin and complexin ensure fast synchronous calcium-evoked neurotransmitter release.
两个相对脂质双层之间同源v-SNARE和t-SNARE的配对驱动自发膜融合，并赋予细胞内膜运输特异性。这些融合事件由一系列蛋白质-蛋白质相互作用调节，这些相互作用局部控制SNARE活性和复合物组装，决定体内何时何地高效发生融合。这种基本调节发生在所有运输步骤，由保守的蛋白质家族介导，如Rab蛋白及其效应器和Sec1/unc18蛋白。受调控的胞吐作用利用辅助成分将信号（触发胞吐作用）与融合机制耦合。在神经元突触处，munc13以及munc18控制SNARE复合物组装。突触结合蛋白和复合物蛋白确保快速同步的钙诱发神经递质释放。
