| Ken Matsuoka | Last modified date：2023.05.17 |
Professor /
Division of Molecular Bioscience
Department of Bioscience and Biotechnology
Faculty of Agriculture
Department of Bioscience and Biotechnology
Faculty of Agriculture
Graduate School
Undergraduate School
Other Organization
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Homepage
https://kyushu-u.pure.elsevier.com/en/persons/ken-matsuoka
Reseacher Profiling Tool Kyushu University Pure
http://www.agr.kyushu-u.ac.jp/lab/plant-nutrition/mat/index.html
Plant Molecular Cell Biology Group, Laboratory of Plant Nutrition .
http://www.agr.kyushu-u.ac.jp/lab/plant-nutrition/
Laboratory of Plant Nutrition .
Phone
092-802-4713
Academic Degree
Doctor of Agriculture
Country of degree conferring institution (Overseas)
No
Field of Specialization
Molecular Cell Biology, Biochemistry, Plant biotechnology
ORCID(Open Researcher and Contributor ID)
0000-0001-7229-7294
Total Priod of education and research career in the foreign country
02years02months
Outline Activities
Researches on the synthesis, modification, transport, localization and degradation of proteins、glycans and complex carbohydrates in plant cells are conducting. Current topics of researches include the regulation mechanism of organelle differentiation, membrane protein localization and degradation under different nutritional conditions, characterization of transport signals, and regulation of protein glycosylation and a valuable glycan synthesis. In addition, researches on the production of valuable plants/crops using genetic engineering and/or environmental control are also conducting.
Research
Research Interests
Membership in Academic Society
- Molecular mechanism of protein and glycan synthesis, transport, localization and modification. Production of useful plants by genetic engineering and environmental control.
keyword : secretory pathway, glycosylation, useful glycan, transport signal, organelle, genetic engineering, environmental control
1991.04Protein localization, modification and degradation.
Papers
| 1. | Kiminori Toyooka, Mayuko Sato, Natsumaro Kutsuna, Takumi Higaki, Fumie Sawaki, Mayumi Wakazaki, Yumi Goto, Seiichiro Hasezawa, Noriko Nagata, Ken Matsuoka, Wide-range High-resolution Transmission Electron Microscopy Reveals Morphological and Distributional Changes of Endomembrane Compartments during Log-to-stationary Transition of Growth Phase in Tobacco BY-2 Cells, Plant Cell Physiol., 10.1093/pcp/pcu084, 55, 9, 1544-1555, 2014.09, Rapid growth of plant cells by cell division and expansion requires an endomembrane trafficking system. The endomembrane compartments, such as the Golgi stacks, endosome and vesicles, are important in the synthesis and trafficking of cell wall materials during cell elongation. However, changes in the morphology, distribution and number of these compartments during the different stages of cell proliferation and differentiation have not yet been clarified. In this study, we examined these changes at the ultrastructural level in tobacco Bright yellow 2 (BY-2) cells during the log and stationary phases of growth. We analyzed images of the BY-2 cells prepared by the high-pressure freezing/freeze substitution technique with the aid of an auto-acquisition transmission electron microscope system. We quantified the distribution of secretory and endosomal compartments in longitudinal sections of whole cells by using wide-range gigapixel-class images obtained by merging thousands of transmission electron micrographs. During the log phase, all Golgi stacks were composed of several thick cisternae. Approximately 20 vesicle clusters (VCs), including the trans-Golgi network and secretory vesicle cluster, were observed throughout the cell. In the stationary-phase cells, Golgi stacks were thin with small cisternae, and only a few VCs were observed. Nearly the same number of multivesicular body and small high-density vesicles were observed in both the stationary and log phases. Results from electron microscopy and live fluorescence imaging indicate that the morphology and distribution of secretory-related compartments dramatically change when cells transition from log to stationary phases of growth.. |
| 2. | Fumie Saito, Akiko Suyama, Takuji Oka, Takehiko Yoko-o, Ken Matsuoka, Yoshifumi Jigami, Yoh-ichi Shimma, Identification of novel peptidyl serine α-galactosyltransferase gene family in plants, J. Biol. Chem., 10.1074/jbc.M114.553933, 289, 20405-20420, 2014.06, In plants, serine residues in extensin, a cell wall protein, are glycosylated with O-linked galactose. However, the enzyme that is involved in the galactosylation of serine had not yet been identified. To identify the peptidyl serine O-α-galactosyltransferase (SGT), we chose Chlamydomonas reinhardtii as a model. We established an assay system for SGT activity using C. reinhardtii and Arabidopsis thaliana cell extracts. SGT protein was partially purified from cell extracts of C. reinhardtii and analyzed by tandem mass spectrometry to determine its amino acid sequence. The sequence matched the open reading frame XP_001696927 in the C. reinhardtii proteome database, and a corresponding DNA fragment encoding 748 amino acids (BAL63043) was cloned from a C. reinhardtii cDNA library. The 748-amino acid protein (CrSGT1) was produced using a yeast expression system, and the SGT activity was examined. Hydroxylation of proline residues adjacent to a serine in acceptor peptides was required for SGT activity. Genes for proteins containing conserved domains were found in various plant genomes, including A. thaliana and Nicotiana tabacum. The AtSGT1 and NtSGT1 proteins also showed SGT activity when expressed in yeast. In addition, knock-out lines of AtSGT1 and knockdown lines of NtSGT1 showed no or reduced SGT activity. The SGT1 sequence, which contains a conserved DXD motif and a C-terminal membrane spanning region, is the first example of a glycosyltransferase with type I membrane protein topology, and it showed no homology with known glycosyltransferases, indicating that SGT1 belongs to a novel glycosyltransferase gene family existing only in the plant kingdom.. |
| 3. | Maiko Tasaki, Satoru Asatsuma, Ken Matsuoka, Monitoring protein turnover during phosphate starvation-dependent autophagic degradation using a photoconvertible fluorescent protein aggregate in tobacco BY-2 cells., Front. Plant Sci. , doi: 10.3389/fpls.2014.00172, ５, 2014.04, [URL]. |
| 4. | Noboru Yamauchi, Tadashi Gosho, Satoru Asatsuma, Kiminori Toyooka, Toru Fujiwara, Ken Matsuoka, Polarized localization and borate-dependent degradation of the Arabidopsis borate transporter BOR1 in tobacco BY-2 cells, F1000Research, 2, 185, [v1; ref status: indexed, http://f1000r.es/kv], 2013.10, In Arabidopsis the borate transporter BOR1, which is located in the plasma membrane, is degraded in the presence of excess boron by an endocytosis-mediated mechanism. A similar mechanism was suggested in rice as excess boron decreased rice borate transporter levels, although in this case whether the decrease was dependent on an increase in degradation or a decrease in protein synthesis was not elucidated. To address whether the borate-dependent degradation mechanism is conserved among plant cells, we analyzed the fate of GFP-tagged BOR1 (BOR1-GFP) in transformed tobacco BY-2 cells. Cells expressing BOR1-GFP displayed GFP fluorescence at the plasma membrane, especially at the membrane between two attached cells. The plasma membrane signal was abolished when cells were incubated in medium with a high concentration of borate (3 to 5 mM). This decrease in BOR1-GFP signal was mediated by a specific degradation of the protein after internalization by endocytosis from the plasma membrane. Pharmacological analysis indicated that the decrease in BOR1-GFP largely depends on the increase in degradation rate and that the degradation was mediated by a tyrosine-motif and the actin cytoskeleton. Tyr mutants of BOR1-GFP, which has been shown to inhibit borate-dependent degradation in Arabidopsis root cells, did not show borate-dependent endocytosis in tobacco BY-2 cells. These findings indicate that the borate-dependent degradation machinery of the borate transporter is conserved among plant species. - See more at: http://f1000research.com/articles/2-185/#sthash.QeZx1wP2.dpuf. |
| 5. | Moses O. Abiodun, Ken Matsuoka, Evidence that Proliferation of Golgi Apparatus Depends on both de novo Generation from the Endoplasmic Reticulum and Formation from Pre-existing Stacks during the Growth of Tobacco BY-2 Cells., Plant Cell Physiol. , 10.1093/pcp/pct014, 54, 4, 541-554, 2013.04, [URL]. |
| 6. | Toyooka, K., Goto, Y., Asatsuma, S., Koizumi, M., Mitsui, T. and Matsuoka, K., A mobile secretory vesicle cluster involved in mass transport from the Golgi to plant cell exterior., Plant Cell, Apr;21(4):1212-29, 2009.04. |
Presentations
- The Japanese Society of Plant Physiologists
- Japan Society for Bioscience, Biotechnology, and Agrochemistry
- Japan Society for Cell Biology
- The Japanese Biochemical Society
- Japanese Society for Plant Cell and Molecular Biology
- Japanese Society of Agricultural, Biological and Environmental Engineers and Scientists
- The Japanese Society for Carbohydrate Research
- American Society for Cell Biology
- The American Society of Plant Biologists
- 16th research paper award. The society for biotechnology, Japan.
Development of Series of Gateway Binary Vectors, pGWBs, for Realizing Efficient Construction of Fusion Genes for Plant Transformation. JBB Vol.104 No.1 p.34
Tsuyoshi Nakagawa, Takayuki Kurose, Takeshi Hino, Katsunori Tanaka, Makoto Kawamukai, Yasuo Niwa, Kiminori Toyooka, Ken Matsuoka, Tetsuro Jinbo, and Tetsuya Kimura
Educational
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