Centers & Labs

Global Research Cluster

Systems Glycobiology Research Group

Group Director: Naoyuki Taniguchi (M.D., Ph.D.)
Naoyuki  Taniguchi(M.D., Ph.D.)

Over 50% of proteins are glycosylated and glycosylation reaction is one of the most important posttranslational modifications of proteins. The sugar chains have different kinds of function, which we are unable to understand from the research on DNA, RNA and proteins. This project focuses on structure and functions of glycoproteins, and we aim to elucidate (1) abnormality of signaling via membrane receptor glycans, and its underlying mechanism of diseases, (2) novel metabolic pathway of free glycans and its role in the quality control of glycoproteins, (3) tertiary structures of glycans and their roles in molecular recognition, and to develop (4) single-molecule imaging of glycans. Through the above researches, we will pursue the basic research, which may develop biomarkers and therapeutics of the diseases such as cancer, infectious diseases, life style-related diseases, and neuromuscular degenerative diseases. Through the above researches, we will establish systems glycobiology in order to understand glycan structure and function from integrative and dynamic aspects, which may develop biomarkers and therapeutics of the diseases such as cancer, infectious diseases, life style-related diseases, and neuromuscular degenerative diseases.
Our group collaborates with Max Planck Institute and continuously contributes to the activities of Japan Consortium for Glycobiology and Glycotechnology (JCGG), which is launched to integrate glycobiology and glycotechnology in Japan.

Main Research Field

Biological Sciences

Related Research Fields

Interdisciplinary science and engineering / Chemistry / Engineering / Biology / Medicine, dentistry, and pharmacy

Keywords

  • Glycobiology
  • glycoproteins
  • Structural biology

Selected Publications

  1. Kizuka Y, Funayama S, Shogomor H, Nakano M, Nakajima K, Oka R, Kitazume S, Yamaguchi Y, Sano M, Korekane H, Hsu T-L, Lee H-Y, Wong C-H and Taniguchi N.
    "Novel Fucose Analog for the High-sensitive Detection of Glycans"
    Cell Chem. Biol. 23, 782-92. (2016)
  2. T. Suzuki, C. Huang and H. Fujihira
    "The cytoplasmic peptide:N-glycanase (NGLY1); structure, expression and cellular functions"
    Gene 577, 1-7. (2016)
  3. T. Suzuki
    "Catabolism of N-glycoproteins in mammalian cells: Molecular mechanisms and genetic disorders related to the processes"
    Mol. Aspects Med. 51, 89-103. (2016)
  4. Kizuka Y, Kitazume S *, Fujinawa R, Saito T, Iwata N, Saido T. C, Nakano M, Yamaguchi Y, Hashimoto Y, Staufenbiel M, Hatsuta H, Murayama S, Manya H, Endo T, and Taniguchi N.
    "An aberrant sugar modification of BACE1 blocks its lysosomal targeting in Alzheimer’s disease"
    EMBO Mol. Med. 15, 175-189. (2015)
  5. Y. Harada, H. Hirayama and T. Suzuki
    "Generation and degradation of free asparagine-linked glycans"
    Cell Mol. Life Sci. 72, 2509-2533. (2015)
  6. Nagae, M., and Yamaguchi, Y.
    "Sugar recognition and protein–protein interaction of mammalian lectins conferring diverse functions"
    Curr Opin Struct Biol., 34, 108-115 (2015)
  7. Kitazume S, Imamaki R, Kurimoto A, Ogawa K, Kato M, Yamaguchi Y, Tanaka K, Ishida H, Ando H, Kiso M, Hashii N, Kawasaki N, and Taniguchi N.
    "Interaction of platelet endothelial cell adhesion molecule (PECAM) with α2,6-sialylated glycan regulates its cell surface residency and anti-apoptotic role"
    J. Biol. Chem. 289, 27606-27613. (2014)
  8. Yamaguchi, Y., Yamaguchi, T., and Kato, K.
    "Structural Analysis of oligosaccharides and glycoconjugates using NMR"
    Adv Neurobiol., 9, 165-83 (2014)
  9. Nagae, M., and Yamaguchi, Y.
    "Three-dimensional structural aspects of protein-polysaccharide interactions"
    Intl J Mol Sci., 15(3), 3768-83 (2014)
  10. Kanekiyo K, Inamori K, Kitazume S, Sato K, Maeda J, Higuchi M, Kizuka Y, Korekane H, Matsuo I, Honke K, and Taniguchi N.
    "Loss of branched O-mannosyl glycans in astrocytes accelerates remyelination"
    J Neurosci. 33, 10037-10047. (2013)

Organization