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.

TANGO1 creates a barrier to control lipid and protein flux across fused secretory compartments.

Novel disease pathways underlie disease pathogenesis in Kelch-related nemaline myopathy through proteomic remodeling.

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.

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.

Upon AMPK activation by acute glucose restriction, Atg14p shifts its distribution from ER exit sites to liquid-ordered membrane domains on the vacuolar surface where, together with Atg6p, it facilitates LD-specific autophagy (i.e., microautophagy of lipid droplets) for energy production and long-term survival of starved cells.

A novel folding machinery assists transmembrane proteins from the cytosolic side of the endoplasmic reticulum.

The coordination of protein targeting to the endoplasmic reticulum and the unfolded protein response through the stress sensor IRE1 ensures quality control of the secreted and transmembrane proteomes.

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

Unconventional secretion of a plasma membrane purine transporter via Golgi-bypass is established at an early ER-associated secretory compartment revealing that specific cargoes define alternative trafficking routes.