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.

Cryo-electron tomography of COPI vesicles in the Golgi reveals coat structure, disassembly dynamics, cargo binding, and morphological variability.

A missing link between the AP complexes and COPI sheds light on the evolution of vesicle coat proteins and trafficking pathways in the earliest eukaryotes.

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

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.

Inactivation of the COPI vesicle coat in yeast reveals that COPI recycles early but not late Golgi proteins.

The ability of COPI to bind polyubiquitin is a key determinant for SNARE incorporation into intracellular vesicles and for maintenance of a functional Golgi complex.

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.

Association of curvature generating proteins to the Golgi membranes by sphingomyelin metabolism essentially controls the flatness of a Golgi cisterna that is necessary for efficient sorting and export.

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