Building on previous work (Diao et al., 2012), we show that the mechanism by which complexin suppresses spontaneous fusion is distinct from the mechanism by which it synchronizes Ca2+-triggered fusion.
Biophysical and functional data strongly support the notion that Munc18-1 acts as a template to assemble the neuronal SNARE complex, and that inhibition of this activity underlies diverse forms of regulation of neurotransmitter release.
The crystal structure of a large C-terminal fragment of Munc13-1 provides a key framework to understand how Munc13-1 mediates neurotransmitter release and presynaptic plasticity.
Sec14l3/SEC14L2 respond to upstream Wnt/Frizzled/Dvl stimulation to recruit and activate phospholipase Cδ4a (Plcδ4a) to further initiate calcium release.
Protein kinase C brings about post-tetanic potentiation - a temporary increase in synaptic strength due to increased transmitter release - via phosphorylation of a target protein, Munc18-1.
Electron-cryomicroscopy structures of the supercomplex of NSF, αSNAP, and neuronal SNAREs in the presence of ATP under non-hydrolyzing conditions at 3.9 Å resolution reveal interactions between the N-terminal residues of SNAP-25 and NSF.