{Reference Type}: Journal Article
{Title}: Regulated exocytosis and SNARE function (Review).
{Author}: Söllner TH;
{Journal}: Mol Membr Biol
{Volume}: 20
{Issue}: 3
{Year}: Jul-Sep 2003
暂无{DOI}: 10.1080/0968768031000104953
{Abstract}: 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.