The first reconstitution of an unconventional secretory mechanism uncovered the molecular mechanism by which Fibroblast Growth Factor 2 is secreted from mammalian cells.

The complex process of protein translocation across membranes has been dissected into multiple key steps and the distributions of translocation rates indicate stochastic nature of the reaction.

Principal curvature-dependent motion of bacterial actin MreB results in localization consistent with all known literature.

Identification of a heparan sulfate proteoglycan with a dedicated function in unconventional protein secretion reveals an intimate relationship between fibroblast growth factor 2 and Glypican-1 in cancer biology.

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

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.

Two domains of the peripheral membrane protein Tim44 interact with two different sectors of a translocase to coordinate the translocation of proteins across the inner mitochondrial membrane.

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 complex that catalyzes the membrane integration of β barrel proteins and a molecular chaperone promote the complete assembly of a bacterial virulence factor in vitro.

Slam is an outer membrane protein translocon that functions with the periplasmic chaperone Skp to translocate protein substrates across the outer membrane of Gram-negative cells.