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.

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.

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

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 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.

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

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

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.

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.

The complex chromatin-based genomic regulatory system controlling developmental gene expression in complex bilaterians predates the evolution of morphological complexity and may have been a prerequisite for the evolution of the first simple multicellular animals.