Synaptotagmin (p65) is an abundant synaptic vesicle protein that contains a single transmembrane region and two copies of an internal repeat that is homologous to the regulatory region of Protein Kinase C. It appears that synaptotagmin has a regulatory role in the synaptic vesicle pathway, particularly in vesicle docking and/or fusion with the plasmalemma. A model has been proposed to explain docking, activation, and fusion of synaptic vesicles with donor membranes. This model suggests that VAMP/synaptobrevin and synaptotagmin (vSNARE) on the synaptic vesicle, and SNAP-25 and syntaxin (tSNAREs) on the plasma membrane, interact to form a 7S complex. Two additional soluble proteins, αSNAP and NSF, are later added to the 7S complex, accompanied by the loss of synaptotagmin. The resulting 20S complex contains syntaxin, SNAP-25, VAMP, αSNAP, and NSF. Genetic studies in several species demonstrate that mutation or deletion of synaptotagmin results in a large decrease in Ca2+ triggered transmitter release. Mammalian synapses that lack synaptotagmin show a selective decrease in a fast component of release, suggesting that synaptotagmin is the Ca2+ sensor triggering exocytosis.
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