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Cooperative action of synaptotagmin and complexin is needed to arrest all SNARE complexes on a vesicle, and the reversal of the synaptotagmin clamp is sufficient to achieve fast, Ca²⁺-synchronized fusion.

Challenging a widespread model, biophysical and electrophysiological experiments suggest a new mechanism whereby complexins inhibit neurotransmitter release through electrostatic repulsion between their accessory helix and the membranes.

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

Novel insights into the molecular mechanisms underlying neurotransmitter release are provided by all-atom molecular dynamics simulations including SNARE proteins, synaptotagmin-1, complexin-1, a vesicle and a flat bilayer.

Biochemical experiments provide support for the trans insertion model for clamping in the regulation of neurotransmitter release by complexin.

Two acidic membrane lipids increase synaptotagmin-1 dwell time and penetration into the membrane, reducing the membrane dissociation of synaptotagmin-1.

When the Ca²⁺-binding loops of the C2B domain insert into a membrane, interactions with a phospholipid and the SNARE complex allow synaptotagmin-1 to bend the membrane.

Calcium-binding synaptotagmins are involved in ring oligomer formation, which allows synaptotagmins to synchronize neurotransmitter release to Ca²⁺ influx.

The analytic theory establishes the general principles of synaptic transmission, enables extraction of microscopic parameters of synaptic fusion machinery from experiments, and links molecular constituents to synaptic function.

Uso1 critically regulating traffic in the ER/Golgi interface is a coiled-coil protein traditionally regarded as a tether, but a forward genetic screen revealed that its essential role appears to involve its ability to interact with SNAREs.