At the ends of their tethers! How coiled-coil proteins capture vesicles at the Golgi.

Cells face a complex problem: how to transfer lipids and proteins between membrane compartments in an organized, timely fashion. Indeed, many thousands of membrane and secretory proteins must traffic out of the ER to different organelles to function, while others are retrieved from the plasma membrane having fulfilled their roles [Nat. Rev. Mol. Cell Biol. (2013) 14 , 382–392]. This process is highly dynamic and failure to target cargo accurately leads to catastrophic consequences for the cell, as is clear from the numerous human diseases associated with defects in membrane trafficking [Int. J. Mol. Sci. (2013) 14 , 18670–18681; Traffic (2000) 1 , 836–851]. How then does the cell organize this enormous transfer of material in its crowded internal environment? And how specifically do vesicles carrying proteins and lipids recognize and fuse with the correct compartment?