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.

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.

The ERK8 kinase blocks the export of glycosyl-tranferases from the Golgi to the endoplasmic reticulum, and thus subsequent O-glycosylation of proteins that otherwise enhance cell motility and tissue invasion.

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

The targeting of proteins from the endoplasmic reticulum to lipid droplets relies on surface modulation of the lipid droplet by the Arf1/COPI machinery.

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.

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

A model-based approach for modelling the immune control of viral dynamics is applied to quantify the effect of several SARS-CoV-2 vaccine platforms and to define mechanistic correlates of protection.

A cross-linking screen finds proteins that interact with TANGO1 to export Procollagen VII, and suggests a new model for the secretion of these bulky cargoes that are involved in skin and bone formation.