A combination of advanced optical imaging and cryogenic electron microscopy has been used to explore membrane fusion in a synthetic system and provide new insights into neurotransmitter release.

Long-lived intermediate states formed by glycoprotein catalysts are an essential part of the process used by influenza virus particles to infect cells.

COPII vesicles regulate the metabolism of cholesterol through the selective transport of secretory proteins.

Experiments on synthetic models of synaptic vesicles have shed new light on the role of the protein α-synuclein in the central nervous system.

C. elegans exhibits two distinct behavioural macro-states, active and quiet wakefulness, and protein kinase A regulates switching between these two states.

α-SNAP mediated rearrangement of Stim1 and Orai1 molecules within CRAC channel clusters is required for store-operated calcium entry.

A cell-free biochemical assay for protein lipidation identifies the ER–Golgi intermediate compartment as a key early station in the formation of an autophagosome.

Long and short variants of a protein called UNC-13, assisted by another called Tomosyn, regulate the timing of synaptic vesicle release in C. elegans.

Optogenetics has revealed that synaptic vesicles can be recycled extremely rapidly in nematodes, indicating that existing models for how synapses 'reload' may need to be revised.

A structure of the complete, membrane bound, COPII coat solved by sub-tomogram averaging reveals the arrangement of all protein subunits on the membrane and suggests a mechanism for coating heterogeneously-shaped carriers.