Recent studies indicate that the molecular machinery for synaptic vesicle docking and fusion consists of a triad of botulinum/tetanus neurotoxin substrates (synaptobrevin, syntaxin, SNAP-25) that are homologues of proteins required for constitutive secretion. Proposed low-affinity Ca2+ sensors that regulate exocytosis remain to be identified, although recent studies on synaptotagmin suggest that it, along with other proteins, could play this role. Regulated peptide secretion from dense-core granules has been found to utilize a similar machinery for docking/fusion, and recent studies indicate that this pathway involves a pre-docking step that is regulated by a higher affinity Ca2+ sensor.