SNARE molecules indicate the complexity of the post-Golgi traffic in plant cells
 
Tomohiro Uemura
Department of Dynamics of Natural Environment, Graduate School of Human and Environmental Studies, Kyoto University, Kyoto 606-8501 Japan
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Although the endomembrane system is well conserved among all eukaryotic cells, the plant endomembrane system also has unique features. In mammals and yeast, each cell has only one type of vacuole, whereas plant cells possess two-types of functionally different vacuoles, a lytic vacuole and a protein storage vacuole. The lytic vacuole is comparable to the mammalian lysosome and the yeast vacuole with an acidic pH of inside of the compartment, while protein storage vacuole is the specialized vacuoles having the capacity to store proteins in seed or vegetative cells. Therefore, protein sorting in plant cells is likely to be more complicated than other eukaryotes because two separate pathways diverge from the Golgi apparatus or plasma membrane to two different vacuole destinations.
In all eucaryotic cells, specific vesicle fusion during vesicular transport is mediated by membrane-associated proteins called SNAREs ( soluble N-ethyl-maleimide sensitive factor attachment protein receptors). In the Arabidopsis genome, 54 SNARE and 57 Rab GTPase genes have been identified. These numbers are greater than those of yeast and mammalians, indicating the complexity of the plant endomembrane system. SNAREs and Rab GTPase are necessary for plant-unique higher order physiological function, suggesting that plants have adopted the membrane trafficking system to plant specific phenomenon.
A series of transient expression assays using green fluorescent protein (GFP) fused proteins revealed that most of SNARE proteins were located on specific intracellular compartments: 6 in the endoplasmic reticulum, 9 in the Golgi apparatus, 4 in the trans-Golgi network (TGN), 2 in endosomes, 17 on the plasma membrane, 7 in both the prevacuolar compartment (PVC) and vacuoles, 2 in TGN/PVC/vacuoles, and 1 in TGN/PVC/plasma membrane. S ome SNARE proteins showed multiple localization patterns in two or more different organelles, suggesting that these SNAREs shuttle between the organelles. Furthermore, the SYP41/SYP61-residing compartment, which we define as the TGN, was not always located along with the Golgi apparatus, suggesting that this compartment is an independent organelle distinct from the Golgi apparatus. We will discuss possible combinations of SNARE proteins on all subcellular compartments, and suggest the complexity of the post-Golgi membrane traffic in higher plant cells.
 
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