佐藤 匡史（サトウ　タダシ）

佐藤 匡史
学位
博士（生物資源科学）
所属・職位
名古屋市立大学 大学院薬学研究科
准教授
URL
http://www.phar.nagoya-cu.ac.jp/hp/sbk/
研究分野
生物物理学、構造生物学、糖鎖生物学

原著論文

  1. Yagi-Utsumi M, Sikdar A, Kozai T, Inoue R, Sugiyama M, Uchihashi T, Yagi H, Satoh T, Kato K.
    Conversion of functionally undefined homopentameric protein PbaA into a proteasome activator by mutational modification of its C-terminal segment conformation.
    Protein Eng. Des. Sel. 31, 29-36 (2018).
  2. Kozai T, Sekiguchi T, Satoh T, Yagi H, Kato K, Uchihashi T.
    Two-step process for disassembly mechanism of proteasome α7 homo-tetradecamer by α6 revealed by high-speed atomic force microscopy.
    Sci. Rep. 7, 15373 (2017).
  3. Sakae Y, Satoh T, Yagi H, Yanaka S, Yamaguchi T, Isoda Y, Iida S, Okamoto Y, Kato K.
    Conformational effects of N-glycan core fucosylation of immunoglobulin G Fc region on its interaction with Fcγ receptor IIIa.
    Sci. Rep. 7, 13780 (2017).
  4. Satoh T, Song C, Zhu T, Toshimori T, Murata K, Hayashi Y, Kamikubo H, Uchihashi T, Kato K.
    Visualisation of a flexible modular structure of the ER folding-sensor enzyme UGGT.
    Sci. Rep. 7, 12142 (2017).
  5. Kurimoto E, Satoh T, Ito Y, Ishihara E, Okamoto K, Yagi-Utsumi M, Tanaka K, Kato K.
    Crystal structure of human proteasome assembly chaperone PAC4 involved in proteasome formation.
    Protein Sci. 26, 1080-1085 (2017).
  6. Suzuki T, Kajino M, Yanaka S, Zhu T, Yagi H, Satoh T, Yamaguchi T, Kato K.
    Conformational analysis of a high-mannose-type oligosaccharide displaying glucosyl determinant recognised by molecular chaperones using NMR-validated molecular dynamics simulation.
    ChemBioChem 18, 396-401 (2017).
  7. Satoh T, Toshimori T, Noda M, Uchiyama S, Kato K.
    Interaction mode between catalytic and regulatory subunits in glucosidase II involved in ER glycoprotein quality control.
    Protein Sci. 25, 2095-2101 (2016).
  8. Satoh T, Toshimori T, Yan G, Yamaguchi T, Kato K. Structural basis for two-step glucose trimming by glucosidase II involved in ER glycoprotein quality control. Sci Rep. 2016 Feb 5;6:20575. doi: 10.1038/srep20575
  9. Ishii K, Noda M, Yagi H, Thammaporn R5, Seetaha S, Satoh T, Kato K, Uchiyama S. Disassembly of the self-assembled, double-ring structure of proteasome α7 homo-tetradecamer by α6. Sci Rep. 2015 Dec 14;5:18167. doi: 10.1038/srep18167
  10. Isoda, Y., Yagi, H., Satoh, T., Shibata-Koyama, M., Masuda, K., Satoh, M., Kato, K. and Iida, S. (2015) Importance of the side chain at position 296 of antibody Fc in interactions with FcγRIIIa and other Fcγ receptors, PLoS One. 2015 Oct 7;10(10):e0140120. doi: 10.1371/journal.pone.0140120. eCollection 2015.
  11. Yagi-Utsumi, M., Satoh, T. and Kato, K. (2015) Structural basis of redox-dependent substrate binding of protein disulfide isomerase, Sci. Rep. 5, 13909.
  12. Inagaki, K., Satoh, T., Yagi-Utsumi, M., Gulluche, A-C.L., Anzai, T., Uekusa, Y., Kamiya, Y. and Kato, K. (2015) Redox-coupled structural changes of the catalytic a' domain of protein disulfide isomerase, FEBS Lett. 589, 2690-2694.
  13. Inagaki, K., Satoh, T., Itoh, S.G., Okumura, H. and Kato, K. (2015) Redox-dependent conformational transition of catalytic domain of protein disulfide isomerase indicated by crystal structure-based molecular dynamics simulation, Chem. Phys. Lett. 618, 203-207.
  14. Zhu, T., Satoh, T. and Kato, K. (2014) Structural insight into substrate recognition by the endoplasmic reticulum folding-sensor enzyme: crystal structure of third thioredoxin-like domain of UDP-glucose:glycoprotein glucosyltransferase, Sci. Rep. 4, 7322.
  15. Satoh, T., Sumiyoshi, A., Yagi-Utsumi, M., Sakata, E., Sasakawa, H., Kurimoto, E., Yamaguchi, Y., Li, W., Joazeiro, C.A., Hirokawa, T. and Kato, K. (2014) Mode of substrate recognition by the Josephin domain of ataxin-3, which has an endo-type deubiquinase activity, FEBS Lett. 588, 4422-4430.
  16. Sikdar, A, Satoh, T., Kawasaki, M. and Kato, K. (2014) Crystal structure of archaeal homolog of proteasome-assembly chaperone PbaA, Biochem. Biophys. Res. Commun. 453, 493-497.
  17. Satoh, T., Saeki, Y., Hiromoto, T., Wang, Y.H., Uekusa, Y., Yagi, H., Yoshihara, H., Yagi-Utsumi, M., Mizushima, T., Tanaka, K., and Kato, K. (2014) Structural basis for proteasome formation controlled by an assembly chaperone Nas2, Structure, 22, 731-743.
  18. Yamamoto, S., Subedi, G.P., Hanashima, S., Satoh, T., Otaka, M., Wakui, H., Sawada, .K, Yokota, S., Yamaguchi, Y., Kubota, H. and Itoh, H. (2014) ATPase activity and ATP-dependent conformational change in the co-chaperone HSP70/HSP90-organizing protein (HOP), J. Biol. Chem. 289, 9880-9886.
  19. Satoh, T., Suzuki, K., Yamaguchi, T. and Kato, K. (2014) Structural basis for disparate sugar-binding specificities in the homologous cargo receptors ERGIC-53 and VIP36, PLoS ONE, 9, e87963.4
  20. Nagae, M., Yamanaka, K., Hanashima, S., Ikeda, A., Morita-Matsumoto, K., Satoh, T., Matsumoto, N., Yamamoto, K., Yamaguchi, Y. (2013) Recognition of bisecting N-acetylglucosamine: structural basis for asymmetric interaction with the mouse lectin dendritic cell inhibitory receptor 2, J. Biol. Chem. 288, 33598-33610.
  21. Kumoi, K., Satoh, T., Murata, K., Hiromoto, T., Mizushima, T., Kamiya, Y., Noda, M., Uchiyama, S., Yagi, H. and Kato, K. (2013) An archaeal homolog of proteasome assembly factor functions as a proteasome activator, PLoS ONE 8, e60294.
  22. Subedi, G.P., Satoh, T., Hanashima, S., Ikeda, A., Nakada, H., Sato, R., Mizuno, M., Yuasa, N., Fujita-Yamaguchi, Y. and Yamaguchi, Y. (2012) Overproduction of anti-Tn antibody MLS128 single-chain Fv fragment in Escherichia coli cytoplasm using a novel pCold-PDI vector, Protein Expr. Purif. 82, 197-204.
  23. Peletskaya, E., Andrake, M., Gustchina, A., Merkel, G., Alexandratos, J., Zhou, D., Bojja, R.S., Satoh, T., Potapov, M., Kogon, A., Potapov, V., Wlodawer, A. and Skalka, A.M. (2011) Localization of ASV integrase DNA contacts by site-directed crosslinking and their structural analysis, PLoS ONE 6, e27751.
  24. Hirano, T., Serve, O., Yagi-Utsumi, M., Takemoto, E., Hiromoto, T., Satoh, T., Mizushima, T. and Kato, K. (2011) Conformational dynamics of wild-type Lys-48-linked diubiquitin in solution, J. Biol. Chem. 286, 37496-37502.
  25. Fujita, M., Watanabe, R., Jaensch, N., Romanova-Michaelides, M., Satoh, T., Kato, M, Riezman, H., Yamaguchi, Y., Maeda, Y., and Kinoshita, T. (2011) Sorting of GPI-anchored proteins into ER-exit sites by p24 proteins is dependent on remodeled GPI, J. Cell Biol. 194, 61-75.
  26. Kanagawa, M., Satoh, T., Ikeda, A., Adachi, Y., Ohno, N. and Yamaguchi, Y. (2011) Structural insights into recognition of triple-helical beta-glucan by insect fungal receptor, J. Biol. Chem. 286, 29158-29165.
  27. Kanagawa, M., Satoh, T., Ikeda, A., Nakano, Y., Yagi, H., Kato, K., Kojima-Aikawa, K. and Yamaguchi, Y. (2011) Crystal structures of human secretory proteins ZG16p and ZG16b reveal a Jacalin-related beta-prism fold, Biochem. Biophys. Res. Commun. 404, 201-205.
  28. Satoh, T., Chen, Y., Hu, D., Hanashima, S., Yamamoto, K., Yamaguchi, Y. (2010) Structural basis for oligosaccharide recognition of misfolded glycoproteins by OS-9 in ER-associated degradation, Mol. Cell 40, 905-916.
  29. Satoh, T., Sakata, E., Yamamoto, S., Yamaguchi, Y., Sumiyoshi, A., Wakatsuki, S. and Kato, K. (2010) Crystal structure of cyclic Lys48-linked tetraubiquitin, Biochem. Biophys. Res. Commun. 400, 329-333.
  30. Satoh, T., Li, M., Nguyen, J.T., Kiso, Y., Gustchina, A and Wlodawer, A. (2010) Crystal structures of inhibitor complexes of human T-cell leukemia virus (HTLV-1) protease, J. Mol. Biol. 401, 626-641.
  31. Sakata, E., Satoh, T., Yamamoto, S., Yamaguchi, Y., Yagi-Utsumi, M., Kurimoto, E., Tanaka, K., Wakatsuki, S. and Kato, K. (2010) Crystal structure of UbcH5b~ubiquitin intermediate: Insight into the formation of the self-assembled E2~Ub conjugate, Structure 18, 138-147.
  32. Satoh, T., Cowieson, N.P., Hakamata, W., Ideo, H., Fukushima, K., Kurihara, M., Kato, R., Yamashita, K. and Wakatsuki, S. (2007) Structural basis for recognition of high mannose type glycoproteins by mammalian transport lectin VIP36, J. Biol. Chem. 282, 28246-28255.
  33. Chida, H., Nakazawa, A., Akazaki, H., Hirano, T., Suruga, K., Ogawa, M., Satoh, T., Kadokura, K., Yamada, S., Hakamata, W., Isobe, K., Ito, T., Ishii, R., Nishio, T., Sonoike, K. and Oku, T. (2007) Expression of the algal cytochrome c6 gene in Arabidopsis enhances photosynthesis and growth, Plant Cell Physiol. 48, 948-957.
  34. Hiraki, M., Kato, R., Nagai, M., Satoh, T., Hirano, S., Ihara, K., Kudo, N., Nagae, M., Kobayashi, M., Inoue, M., Uejima, T., Oda, S., Chavas, L.M., Akutsu, M., Yamada, Y., Kawasaki, M., Matsukgaki, N., Igarashi, N., Suzuki, M. and Wakatsuki, S. (2006) Development of an automated large scale protein crystallization and monitoring system for high-throughput protein structure analyses, Acta Crystallogr. D62, 1058-1065.
  35. Chida, H., Yokoyama, T., Kawai, F., Nakazawa, A., Akazaki, H., Takayama,Y., Hirano, T., Suruga, K., Satoh, T., Yamada, S., Kawachi, R., Unzai, S., Nishio, T., Park, S.-Y. and Oku, T. (2006) Crystal structure of oxidized cytochrome c6A from Arabidopsis thaliana, FEBS Lett. 580, 3763-3768.
  36. Satoh, T., Sato, K., Kanoh, A., Yamashita, K., Yamada, Y., Igarashi, N., Kato, R., Nakano, A. and Wakatsuki, S. (2006) Structures of the carbohydrate recognition domain of Ca2+-independent cargo receptors Emp46p and Emp47p, J. Biol. Chem. 281, 10410-10419.
  37. Suruga, K., Murakami, K., Taniyama, Y., Hama, T., Chida, H., Satoh, T., Yamada, S., Hakamata, W., Kawachi, R., Isogai, Y., Nishio, T. and Oku, T. (2004) A novel microperoxidase activity: methyl viologen-linked nitrite reducing activity of microperoxidase, Biochem. Biophys. Res. Commun. 315, 815-822.
  38. Suruga, K., Nagasawa, N., Yamada, S., Satoh, T., Kawachi, R., Nishio, T., Kume, T. and Oku, T. (2003) Radiation-induced enhancement of nitrite reducing activity of cytochrome c, J. Agric. Food Chem. 51, 6835-6843.
  39. Yamada, S., Suruga, K., Ogawa, M., Hama, T., Satoh, T., Kawachi, R., Nishio, T. and Oku, T. (2002) Appearance of nitrite reducing activity of cytochrome c upon heat denaturation, Biosci. Biotechnol. Biochem. 66, 2044-2051.
  40. Satoh, T., Itoga, A., Isogai, Y., Kurihara, M., Yamada, S., Natori, M., Suzuki, N., Suruga, K., Kawachi, R., Arahira, M., Nishio, T., Fukazawa, C. and Oku, T. (2002) Increasing the conformational stability by replacement of heme axial ligand in c-type cytochrome, FEBS Lett. 531, 543-547.
  41. Yamada, S., Park, S.-Y., Shimizu, H., Koshizuka, Y., Kadokura, K., Satoh, T., Suruga, K., Ogawa, M., Isogai, Y., Nishio, T., Shiro, Y. and Oku, T. (2000) Structure of cytochrome c6 from the red alga Porphyra yezoensis at 1.57 Å resolution, Acta Crystallogr. D56, 1577-1582.
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総説等

  1. Zhang, Y., Yamaguchi, T., Satoh, T., Yagi-Utsumi, M., Kamiya, Y., Sakae, Y., Okamoto, Y. and Kato, K. (2015) Conformational dynamics of oligosaccharides characterized by paramagnetism-assisted NMR spectroscopy in conjunction with molecular dynamics simulation, Adv. Exp. Med. Biol. 842, 217-230.
  2. Kamiya, Y., Satoh, T. and Kato, K. (2014) Recent advances in glycoprotein production for structural biology: toward tailored design of glycoforms, Curr. Opin. Struct. Biol. 26, 44-53.
  3. Satoh, T. (2012) Molecular and structural basis for sugar recognition by mannose 6-phosphate receptor homology domain-containing lectins and proteins, Trends Glycosci. Glycotechnol. 24, 193-202.
  4. Kamiya, Y., Satoh, T. and Kato, K. (2012) Molecular and structural basis for N-glycan-dependent determination of glycoprotein fates in cells, Biochim. Biophys. Acta. 1820, 1327-1337.
  5. Satoh, T., Yamaguchi, T. and Kato, K. (2015) Emerging structural insights into glycoprotein quality control coupled with N-glycan processing in the endoplasmic reticulum, Molecules 20, 2475-2491.
  6. 佐藤匡史，山口芳樹（2012）糖鎖を目印とするタンパク質の品質管理の仕組みを解く，生物物理 52(1), 32-33.
  7. 坂田絵理，佐藤匡史，山口芳樹，若槻壮市，加藤晃一(2010) 細胞の中の不要なタンパク質に目印をつける仕組み，日本結晶学会誌 52, 255-261.
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