The function and distribution of kinesin motors on exocytotic vesicles is dissected and visualized through a combination of gene knockout experiments, high-resolution microscopy and advanced data analysis.

Evidence that certain proteins can be transported between Golgi via structures that resemble COPI vesicles suggests that these vesicles could also be involved in the transport of proteins from the cis to the trans face of the Golgi.

Components of a Spir:MyoV:Rab11 complex are recruited synergistically to coordinate actin tracks generation and myosin motor activity in vesicle transport processes.

In mammals, the vesicular glutamate transporter 1 acquired a proline-rich sequence that negatively regulates the spontaneous release of glutamate by reducing the exchange of synaptic vesicles along the axon.

The golgin GMAP-210 captures vesicles at the cis Golgi by merely recognizing the high curvature and lipid unsaturation level of transport vesicles.

The COPII coat protein, in association with p24 machinery molecules, actively excludes misfolded and resident proteins from endoplasmic reticulum-derived transport vesicles.

A fear conditioning-induced miRNA acts in a negative feedback loop that targets vesicle exocytosis and neurotransmitter receptor trafficking, and inhibits memory formation.

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.

Whole endosome recording shows that chloride interacts with vesicular glutamate transporters as both allosteric activator and permeant ion, and although the mode of permeation differs, chloride and glutamate use a related conduction pathway.

In central synapses, the mobility and supply of synaptic vesicles are determined by two independent biological factors: the morphological and structural organization of nerve terminals and the molecular signature of vesicles.