Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum.

Newly synthesized proteins are believed to move from the endoplasmic reticulum (ER) to the Golgi by bulk flow, and sorting is assumed to occur exclusively in the trans-Golgi network (TGN). Using quantitative immunoelectron microscopy, we demonstrate that vesicular stomatitis virus glycoprotein (VSV-G) is sorted from resident ER proteins and concentrated 5- to 10-fold in 40-80 nm vesicles during vesicle budding from the ER. Accumulation of VSV-G in pre-Golgi vesicular carriers is the only detectable concentration step in its transport to the TGN. From these results, it is apparent that export from the ER is not exclusively mediated by bulk flow. The ER exerts an unanticipated level of control to insure selective and efficient entry of mature protein into the secretory pathway.