Synaptotagmin 7 is asymmetrically localized to the axonal plasma membrane through γ-secretase processing to promote vesicle docking during short-term synaptic plasticity in mouse hippocampal neurons.

A novel region in the CaV2.1 α1 subunit regulates coupling of synaptic vesicles to CaV2.1 calcium channels, synaptic vesicle release and docking, and the size of the fast and total releasable pools of synaptic vesicles.

SNX4 influences synaptic vesicle recruitment at the active zone, linking endosomal sorting to docked vesicle density and modulating neurotransmission efficiency during sustained activity.

Munc13 C-terminal domains synergize to coordinate synaptic vesicle docking, priming and fusion.

Munc13 proteins are key determinants of large dense-core vesicle (LDCV)-dependent catecholamine release in chromaffin cells.

Cryo-electron tomography, reconstitution, and electrophysiological data show that a fundamental function of Munc13-1 is to bridge synaptic vesicles to the presynaptic plasma membrane.

The probability of occupancy of individual synaptic release sites at rest sets an upper limit to synaptic output when increasing action potential related calcium entry.

Stationary dense-core vesicles depend on the CAPS-1 protein to fuse with the presynaptic membrane.

Parallel measurements of pH gradient and membrane potential at the single vesicle level have revealed that the synaptic vesicle acidification is initiated by removal of its clathrin coat, which blocks vesicular ATPase activity.

The calcium-binding proteins synaptotagmin 7 and Doc2α act sequentially during asynchronous neurotransmitter release.