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First published online May 28, 2008; 10.1104/pp.108.119925 Plant Physiology 147:1637-1645 (2008) © 2008 American Society of Plant Biologists OPEN ACCESS ARTICLE
SCAMPs Highlight the Developing Cell Plate during Cytokinesis in Tobacco BY-2 Cells1,[C],[W],[OA]Department of Biology and Molecular Biotechnology Program, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China (S.K.L., Y.C., L.J.); and Department of Cell Biology, Heidelberg Institute for Plant Sciences, University of Heidelberg, D–69120 Heidelberg, Germany (S.H., D.G.R.)
We previously demonstrated that rice (Oryza sativa) SECRETORY CARRIER MEMBRANE PROTEIN1 (OsSCAMP1)-yellow fluorescent protein in transgenic tobacco (Nicotiana tabacum) Bright Yellow-2 cells locates to the plasma membrane and to motile punctate structures, which represent the trans-Golgi network/early endosome and are tubular-vesicular in nature. Here, we now show that SCAMPs are diverted to the cell plate during cytokinesis dividing Bright Yellow-2 cells. As cells progress from metaphase to cytokinesis, punctate OsSCAMP1-labeled structures begin to collect in the future division plane. Together with the internalized endosomal marker FM4-64, they then become incorporated into the cell plate as it forms and expands. This was confirmed by immunogold electron microscopy. We also monitored for the Golgi apparatus and the prevacuolar compartment (PVC)/multivesicular body. Golgi stacks tend to accumulate in the vicinity of the division plane, but the signals are clearly separate to the cell plate. The situation with the PVC (labeled by green fluorescent protein-BP-80) is not so clear. Punctate BP-80 signals are seen at the advancing periphery of the cell plate, which was confirmed by immunogold electron microscopy. Specific but weak labeling was observed in the cell plate, but no evidence for a fusion of the PVC/multivesicular body with the cell plate could be obtained. Our data, therefore, support the notion that cell plate formation is mainly a secretory process involving mass incorporation of domains of the trans-Golgi network/early endosome membrane. We regard the involvement of multivesicular late endosomes in this process to be equivocal.
1 This work was supported by grants from the Research Grants Council of Hong Kong (grant nos. CUHK4307/03M, CUHK4580/05M, and CUHK488707), UGC-AoE, Chinese University of Hong Kong Scheme C, National Science Foundation of China (grant no. 30529001), and the National 863 Program of China (grant no. 2007AA02Z102) to L.J. and from the Deutsche Forschungsgemeinschaft to D.G.R. The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Liwen Jiang (ljiang{at}cuhk.edu.hk). [C] Some figures in this article are displayed in color online but in black and white in the print edition. [W] The online version of this article contains Web-only data. [OA] Open Access articles can be viewed online without a subscription. www.plantphysiol.org/cgi/doi/10.1104/pp.108.119925 * Corresponding author; e-mail ljiang{at}cuhk.edu.hk. Received March 27, 2008; accepted May 19, 2008; published May 28, 2008. This article has been cited by other articles:
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