Biochemical studies in combination with computational modeling and molecular dynamics simulations reveal that the lipid bilayer promotes intramembrane proteolysis by stabilizing the enzyme-substrate complex and the protease active site.

A novel mechanism of intramembrane protease regulation involves a protein blocking the active site of the enzyme.

The import of proteins into the intermembrane space of mitochondria is driven by binding to the trans-site receptor Mia40 and not by the oxidation of cysteine residues.

Intramembrane proteases identify target proteins in a different way from other proteases.

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

Mutational analysis and biochemical experiments suggest that the conserved β-hairpin-like membrane-reentrant loop of RseP - an S2P family intramembrane cleaving protease - helps to discriminate substrates by directly interacting with their transmembrane segments.

Structural and biochemical analysis of an abundant and conserved protein complex called EMC shows how it is likely to insert nascent membrane proteins into the endoplasmic reticulum membrane.

Reconstitution of interleukin-1β secretion in non-macrophage cells implicates how this pro-inflammatory cytokine enters into the unconventional pathway of secretion through autophagy.

The conserved polypeptide transport associated (POTRA) domains of the protein import channel, Toc75, are essential for protein import into chloroplasts.

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