Nils Stührwohldt, Stefan Scholl ... Andreas Schaller
Step-wise processing of plant peptide hormone precursors by subtilisin-like proteinases in consecutive compartments of the secretory pathway is required for formation and secretion of the bioactive peptides.
Tolulope Sokoya, Jan Parolek ... Joost CM Holthuis
Organellar lipidomics and lipid reporter studies in intact cells reveal how disease-relevant mutations in a sphingolipid biosynthetic enzyme cause a wide-ranging perturbation of lipid distributions and membrane properties along the secretory pathway.
A pseudokinase in the secretory pathway, Fam20A, activates the real Golgi casein kinase, Fam20C, via a unique mechanism that is lost in human diseases.
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.
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.
ER-resident chaperones and cargo receptors make excursions to the cell surface and endocytic compartments when they accompany misfolded clients to lysosomes for degradation.
Rab26 selectively directs synaptic and secretory vesicles into preautophagosomal structures, suggesting the presence of a novel pathway (vesiculophagy) for degradation of synaptic vesicles.