Super-resolution microscopy sets a new strategy to comprehend the membrane organization of γ-secretase at single complex resolution identifying nanodomain associations and its diffusion in situ in the living membrane.

Genetic rescue experiments reveal that γ-secretase enzymes containing Aph1b subunits control signalling by type III neuregulin 1, with implications for schizophrenia.

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

HID-1 is a novel player mediating homotypic fusion of immature secretory granules.

A masked cryo-EM image classification approach and the structure of an inhibitor-bound complex provide insights into the molecular flexibility of the catalytic subunit of gamma-secretase.

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

The structures of secretory and dimeric IgA reveal pseudosymmetric assemblies of two antibody monomers, in which possible positions of antigen-binding fragments and accessibility to receptor-binding sites are limited.

The protease γ-secretase generates amyloid-beta peptides using a mechanism that is driven by the stabilization of an enzyme-substrate scisson complex.