Recycling of Solanum Sucrose Transporters Expressed in Yeast, Tobacco, and in Mature Phloem Sieve Elements  

作　　者：Johannes Liesche Hong-Xia He Bernhard Grimm Alexander Schulz Christina Kuhn 

机构地区：[1]Humboldt University, Institute of Biology, Plant Physiology, Philippstraβe 13, Building 12, 10115 Berlin, Germany [2]Plant Physiology and Anatomy Laboratory, Department of Plant Biology, Faculty of Life Sciences, Copenhagen University, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Denmark

出　　处：《Molecular Plant》2010年第6期1064-1074,共11页分子植物（英文版）

摘　　要：The plant sucrose transporter SUT1 （from Solanum tuberosum, S. lycopersicum, or Zea mays） exhibits redoxdependent dimerization and targeting if heterologously expressed in S. cerevisiae （Krtigel et al., 2008）. It was also shown that SUT1 is present in motile vesicles when expressed in tobacco cells and that its targeting to the plasma membrane is reversible. StSUT1 is internalized in the presence of brefeldin A （BFA） in yeast, plant cells, and in mature sieve elements as confirmed by immunolocalization. These results were confirmed here and the dynamics of intracellular SUT1 localization were further elucidated. Inhibitor studies revealed that vesicle movement of SUT1 is actin-dependent. BFA-mediated effects might indicate that anterograde vesicle movement is possible even in mature sieve elements, and could involve components of the cytoskeleton that were previously thought to be absent in SEs. Our results are in contradiction to this old dogma of plant physiology and the potential of mature sieve elements should therefore be re-evaluated. In addition, SUT1 internalization was found to be dependent on the plasma membrane lipid composition. SUT1 belongs to the detergent-resistant membrane （DRM） fraction in planta and is targeted to membrane raft-like microdomains when expressed in yeast （Kr（igel et al,, 2008）, Here, SUT1-GFP expression in different yeast mutants, which were unable to perform en- docytosis and/or raft formation, revealed a strong link between SUT1 raft localization, the sterol composition and mem- brane potential of the yeast plasma membrane, and the capacity of the SUT1 protein to be internalized by endocytosis. The results provide new insight into the regulation of sucrose transport and the mechanism of endocytosis in plant cells.The plant sucrose transporter SUT1 （from Solanum tuberosum, S. lycopersicum, or Zea mays） exhibits redoxdependent dimerization and targeting if heterologously expressed in S. cerevisiae （Krtigel et al., 2008）. It was also shown that SUT1 is present in motile vesicles when expressed in tobacco cells and that its targeting to the plasma membrane is reversible. StSUT1 is internalized in the presence of brefeldin A （BFA） in yeast, plant cells, and in mature sieve elements as confirmed by immunolocalization. These results were confirmed here and the dynamics of intracellular SUT1 localization were further elucidated. Inhibitor studies revealed that vesicle movement of SUT1 is actin-dependent. BFA-mediated effects might indicate that anterograde vesicle movement is possible even in mature sieve elements, and could involve components of the cytoskeleton that were previously thought to be absent in SEs. Our results are in contradiction to this old dogma of plant physiology and the potential of mature sieve elements should therefore be re-evaluated. In addition, SUT1 internalization was found to be dependent on the plasma membrane lipid composition. SUT1 belongs to the detergent-resistant membrane （DRM） fraction in planta and is targeted to membrane raft-like microdomains when expressed in yeast （Kr（igel et al,, 2008）, Here, SUT1-GFP expression in different yeast mutants, which were unable to perform en- docytosis and/or raft formation, revealed a strong link between SUT1 raft localization, the sterol composition and mem- brane potential of the yeast plasma membrane, and the capacity of the SUT1 protein to be internalized by endocytosis. The results provide new insight into the regulation of sucrose transport and the mechanism of endocytosis in plant cells.

关 键 词：Transporters membrane proteins phloem physiology protein targeting potato. 

分 类 号：Q945.65[生物学—植物学] S572.01[农业科学—烟草工业]