A Distinct Pathway for Polar Exocytosis in Plant Cell Wall Formation.

Post-Golgi protein sorting and trafficking to the plasma membrane (PM) is generally believed to occur via the trans-Golgi network (TGN). In this study using Nicotiana tabacum pectin methylesterase (NtPPME1) as a marker, we have identified a TGN-independent polar exocytosis pathway that mediates cell wall formation during cell expansion and cytokinesis. Confocal immunofluorescence and immunogold electron microscopy studies demonstrated that Golgi-derived secretory vesicles (GDSVs) labeled by NtPPME1-GFP are distinct from those organelles belonging to the conventional post-Golgi exocytosis pathway.

Secretory carrier membrane proteins.

Secretory carrier membrane proteins (SCAMPs) are a family of integral membrane proteins that play roles in mediating exocytosis in animal cells. However, relatively little is known about the subcellular localization, trafficking, and function of SCAMPs in plants. Several recent studies in plant cells indicate that plant SCAMPs share many similarities with their mammalian homologs although there are differences.

BFA-induced compartments from the Golgi apparatus and trans-Golgi network/early endosome are distinct in plant cells.

Brefeldin A (BFA) is a useful tool for studying protein trafficking and identifying organelles in the plant secretory and endocytic pathways. At low concentrations (5-10 microg ml(-1)), BFA caused both the Golgi apparatus and trans-Golgi network (TGN), an early endosome (EE) equivalent in plant cells, to form visible aggregates in transgenic tobacco BY-2 cells. Here we show that these BFA-induced aggregates from the Golgi apparatus and TGN are morphologically and functionally distinct in plant cells.