A novel component of type III protein secretion systems involved in the assembly of the secretion machine is reported.

The release of Acb1 protein from yeast cells requires the ESCRT-III complex to stabilize the compartment for unconventional protein secretion (CUPS).

The time it takes to secrete a protein is dominated by diffusion of positively charged arginines through the channel across the membrane, but lysines avoid this problem as they are neutralised before transport.

A membrane-associated, supramolecular protein complex with dynamically changing components, the central supramolecular activation cluster, regulates the generation of the T cell effector cytokine IL-2 depending on its composition.

Surface protein precursors traffic to lipoteichoic acid-rich septal membranes of Staphylococcus aureus for cleavage of their YSIRK-GXXS motif signal peptides and SecA-mediated translocation across the plasma membrane.

The basal body of the type-III secretion system of Yersinia enterocolitica within bacterial membranes shows elasticity and is longer than related isolated systems.

Hepsin is the first protease identified to modulate specific cleavage and secretion of a Zona Pellucida domain protein, uromodulin.

The Helicobacter pylori Cag T4SS has unique structural features, including unexpected symmetry mismatch between sub-complexes, with implications for protein secretion.

Epithelial tumors secrete the ER-resident AGR2 in the extracellular matrix to function as a novel essential microenvironmental regulator of epithelial tissue architecture, which leads to tumorigenicity.

A widespread family of chaperones functions to stabilize membrane protein effectors by mimicking transmembrane helical environments and promotes effector export by the bacterial type VI secretion system.