Jeff Coleman

This study shows that two Munc13 oligomers are essential for vesicle docking and SNARE assembly, supporting neurotransmitter release.

The paper uses super-resolution microscopy to show golgin proteins form a tetraplex at the Golgi rim and self-assemble into filamentous bands, proposing a model for Golgi stack formation.

This paper introduces a platform for high-throughput extraction of membrane proteins into native nanodiscs while preserving their local membrane context and provides a database for optimized extraction conditions.

This paper identifies Synaptophysin as a chaperone that organizes 12 SNAREpins under each synaptic vesicle through its hexamer structure and VAMP2 dimer binding.

The paper reconstitutes core synaptic machinery to reveal DAG's role in vesicle priming and Ca2+-triggered release, showing DAG accelerates SNAREpin assembly and affects release dynamics.

The paper shows Munc13-1 directly binds SNAP25 to initiate SNARE complex assembly, using FRET and optical tweezer techniques.

This study shows that Syt1 oligomerisation is essential for clamping spontaneous and asynchronous neurotransmitter release, revealing a mechanism for regulating release modes.

This study investigates the independent yet synergistic roles of Synaptotagmin-1 and Complexin in calcium-regulated neuronal exocytosis using a reconstituted single-vesicle fusion assay.

This paper determines the structure of the Syt1-SNARE complex on lipid membranes using cryo-electron microscopy to elucidate how Syt1 clamps and activates SNARE-mediated fusion through Ca2+ and Mg2+ dependent interactions.