Large pleiomorphic traffic intermediates in the secretory pathway.

There are two main classes of traffic intermediates that operate in intracellular trafficking pathways: small round vesicles, and large pleiomorphic carriers (LPCs). While both are essential, the LPCs appear to be responsible for moving the bulk of the secretory traffic between distant compartments. LPCs are much larger and more variable in shape than vesicles, and they have evident interconnected tubular and saccular/cisternal components. They appear to form by en bloc extrusion and cleavage of large membrane areas of the donor organelle. Although many proteins and lipids that are involved in LPC formation have been identified, the intrinsic complexity of these carriers and current technical limitations mean that a coherent picture of the process of of LPC formation is only just beginning to emerge.

CtBP3/BARS drives membrane fission in dynamin-independent transport pathways.

Membrane fission is a fundamental step in membrane transport. So far, the only fission protein machinery that has been implicated in in vivo transport involves dynamin, and functions in several, but not all, transport pathways. Thus, other fission machineries may exist. Here, we report that carboxy-terminal binding protein 3/brefeldin A-ribosylated substrate (CtBP3/BARS) controls fission in basolateral transport from the Golgi to the plasma membrane and in fluid-phase endocytosis, whereas dynamin is not involved in these steps. Conversely, CtBP3/BARS protein is inactive in apical transport to the plasma membrane and in receptor-mediated endocytosis, both steps being controlled by dynamin. This indicates that CtBP3/BARS controls membrane fission in endocytic and exocytic transport pathways, distinct from those that require dynamin.