NSF is part of a membrane trafficking quality control system that disassembles both properly formed and off-pathway SNARE complexes, and the disassembly activity may be regulated by complexin.

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

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.

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.

Isothermal titration calorimetry experiments clarify apparently discrepant results described previously and show that N-terminal sequences of complexin bind to SNARE complexes containing C-terminally truncated synaptobrevin when they include the syntaxin-1 juxtamembrane region.

The far C-terminal domain of CpxII interferes with SNARE assembly and thereby arrests tonic exocytosis.

The use of network science to quantify the properties of global cellular organization in the plant hypocotyl identifies higher-order properties and plasticity in epidermal cell patterning.

A deeply conserved feature of complexin's secondary structure underlies its inhibitory function despite poor primary sequence conservation.

Pupil-linked arousal dynamics are influenced more strongly by high-level internal belief states than by low-level sensory events during decision-making.

Complexin can have two conformations when bound to a ternary SNARE complex, one of which induces a conformational change of the SNARE complex at the C-terminus.