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

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.

Src phosphorylates GBF1, promoting binding of the Sec7 domain to Arf1 and the formation of GALNTs containing tubules emanating from the Golgi.

The amphipathic helix of perilipin 4 relies on the organization of its polar residues to form a remarkably immobile and stable protein layer on the surface of lipid droplets.

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 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.

Amino-acid starvation leads to the formation of a reversible stress assembly, the Sec body, which is a pro-survival reservoir for components of the ER exit sites.

Two cryo-EM structures of the mammalian BBSome show how the BBSome is recruited to membranes and activated by the GTPase ARL6 prior to binding transmembrane proteins.

Transmembrane protein Erd1 and the cytosolic receptor Vps74 cooperate to mediate early Golgi glycosyltransferase recycling in budding yeast.