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

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

Secretion and fibrillogenesis of collagen-I are separately controlled molecular pathways in the fibroblast, where surprisingly endocytic recycling is required for fibril formation and is increased in fibrotic fibroblasts.

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

Building on previous work (Nogueira et al., 2014), we describe a mechanism for the generation of a mega-carrier for the export of bulky procollagen from the endoplasmic reticulum.

Excess membrane can trap outgoing extracellular matrix proteins in secreting cells, leading to pericellular deposits that cause tissue damage.

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.

The cisternae of the Golgi contain two functionally distinct domains: the central areas, which remain stationary, and the edges or rims, which are mobile.

Drosophila ZIP13 (Slc39a13), a presumed zinc importer, is responsible for iron delivery to the secretory pathway.