Parallel measurements of pH gradient and membrane potential at the single vesicle level have revealed that the synaptic vesicle acidification is initiated by removal of its clathrin coat, which blocks vesicular ATPase activity.

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.

A molecular model of the assembled COPI coat, determined by cryo-electron tomography of an in vitro reconstituted budding reaction, reveals details of interactions mediating coat assembly and shows the binding site of ArfGAP2.

TANGO1 functions as a linactant filament to stabilize shallow COPII-coated buds, and after which membrane tension regulation, possibly mediated by TANGO1-controlled membrane fusion, facilitates bud elongation for procollagen export.

A combination of light and electron microscopy data provide new insights into the dynamic architecture and the function of the endocytic protein machinery in relation to membrane shape changes in vivo.

The ability of epithelial cells to distinguish between domains on opposing cell surfaces within a tissue, a property known as planar cell polarity, relies on proteins and protein complexes directing the traffic of signaling proteins to specific locations on the cell surface membrane.

COPI vesicle coat protein recognizes a ubiquitin sorting signal on an exocytic v-SNARE to mediate recycling.

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

Electron tomography and biochemical approaches demonstrate a direct role for WDR35, beyond integrity of the IFT-A holocomplex, in the formation and fusion of electron-dense-coated vesicles to the ciliary sheath and pocket for delivery of cargos necessary for axoneme elongation.