A cell-free biochemical assay for protein lipidation identifies the ER–Golgi intermediate compartment as a key early station in the formation of an autophagosome.

Spatiotemporal mapping of a variety of proteins in and around the Golgi apparatus in budding yeast was performed using super-resolution live imaging microscopy and identified the ER-Golgi intermediate compartment that matures into the Golgi.

Building on previous work (Ge et al., 2013), it is shown that the ER-Golgi intermediate compartment is a platform for the production of COPII vesicles as precursor membranes for the lipidation of LC3, which is an essential step in autophagosome biogenesis.

An unbiased model for the self-organisation of the Golgi apparatus displays either anterograde vesicular transport or cisternal maturation depending on ratios of budding, fusion and biochemical conversion rates.

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.

By partitioning promiscuous enzymes across multiple Golgi compartments, eukaryotic cells can tightly control the synthesis of complex sugar oligomers.

A screen of tens of thousands of vesicle traffic networks in silico shows that Golgi-like cisternal maturation is a natural outcome of vesicle traffic homeostasis.

The first human TANGO1-associated syndromal disease manifests as impaired collagen secretion, highlighting the importance of TANGO1 in human pathophysiology.

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

Death receptor 5 can directly sense misfolded proteins downstream of the endoplasmic reticulum to provide a quality control mechanism that executes apoptosis and prevents further production of misfolded proteins.