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

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.

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

Advances in imaging techniques have shed new light on the structure of vesicles formed by COPI protein complexes.

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.

TANGO1 creates a sub-compartment at the endoplasmic reticulum, to segregate and export fully assembled bulky cargoes.

Erythroid-enriched BMP2K kinase, in addition to its predicted function in endocytosis, regulates distribution and abundance of COPII assemblies and autophagic degradation through opposing actions of its two splicing variants.

Transport machinery localizes at the cisternal rim while modification machinery localizes at the interior.

Ceapins specifically inhibit ATF6α signaling by preventing its transport to the Golgi during endoplasmic reticulum stress.

The control of SEC23B degradation by SCF^FBXW5 and ULK1 regulates the autophagy.