TGN46 is a cargo receptor, with its luminal domain being necessary and sufficient to load soluble secretory proteins into transport carriers for export out of the trans-Golgi network.

Analyses of knockout mice and a biochemical screen of interacting proteins reveal that exophilin-8 forms a large network of protein interactions to efficiently retain secretory granules beneath the plasma membrane for exocytosis.

Neurons use a non-canonical secretory network to deliver select proteins to postsynaptic sites in dendrites.

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.

Targeting senescent cells in human intervertebral discs, using senotherapeutics, provides a potential therapeutic strategy to prevent or reduce disc degeneration and pain.

Novel modelling strategies can integrate the dynamics of processes regulating the intestinal epithelium at multiple scales in homeostasis and following perturbations to provide unprecedented insights into the biology of the epithelium and support the development of safer novel drug candidates.

A receptor protein called TGN46 has an important role in sorting secretory proteins into vesicles going to different destinations inside cells.

Gradual downregulation of each of the subunits of the evolutionary-conserved exocyst holocomplex shows that the complex is required for biogenesis, maturation, and exocytosis of secretory granules in Drosophila salivary glands.

TIRF microscopy in living pancreatic beta cells lacking one or two of Rab27 effectors and the exocyst components reveals how each molecule functions in sequence or in parallel in multiple redundant paths and rate-limiting processes in granule exocytosis.

The viscous hydraulics of contracting endoplasmic reticulum networks challenge common solute transport theories, suggesting the contraction of peripheral sheets as a plausible driving mechanism.