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Laboratory for Protein Conformation Diseases
Motomasa TANAKA
Laboratory Head
Motomasa TANAKA (Ph.D.)
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Research Areas

We search for novel functional amyloids and analyze their physiological roles in cells. We also investigate molecular basis of mental disorders and neurodegenerative diseases using a variety of methods including chemical biology, genetics, structural biology and neurobiology. Furthermore, we aim to reveal structural basis of yeast prion strains and transmission barriers.

Research Subject

  1. Analysis of novel functional amyloid
  2. Molecular basis of mental disorders
  3. Protein misfolding and neurodegenerative diseases
  4. Structural basis of yeast prion strains and transmission barriers

Related links

  1. RIKEN Brain Science Institute Website_Laboratories PageNew Window

Press release

January 18, 2010
Effect of yeast prion protein oligomer formation process on infection efficacy clarified
May 26, 2009
Differences in protein coagulation structure contribute to the onset of Huntington's disease. The degree of toxicity is found to be regulated by proteins in the same amino acid configuration forming different amyloidal structures.

RIKEN RESEARCH

April 02, 2010
Unfolding the genesis of 'bad' seeds
Specific characteristics of small clumps of prion proteins dictate the conformation of larger aggregates that could influence disease symptomsNew Window
July 31, 2009
A slight twist with serious consequences
Subtle structural changes can markedly affect one protein's toxic impact, and may help explain the distinctive pathology of Huntington's diseaseNew Window

List of Selected Publications

  1. Tonoki, A., Kuranaga, E., Ito, N., Nekooki-Machida, Y., Tanaka, M., Miura, M.
    Aging causes distinct characteristics of polyglutamine amyloids in vivo.
    Genes Cells 16, 557-564 (2011).
  2. Foo, C.K., Ohhashi, Y., Kelly, M.J., Tanaka, M., Weissman, J.S.
    Radically Different Amyloid Conformations Dictate the Seeding Specificity of a Chimeric Sup35 Prion.
    J. Mol. Biol. 408, 1-8 (2011).
  3. Ohhashi, Y., Ito, K., Toyama, BH, Weissman, JS., and Tanaka, M.:
    "Differences in prion strain conformations result from non-native interactions in a nucleus."
    Nature Chem. Biol., 6, 225-230 (2010).
  4. Nekooki-Machia, Y., Kurosawa, M., Nukina, N., Ito, K, Oda, T., and Tanaka, M..:
    "Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity."
    Proc. Natl. Acad. Sci. U. S. A., 106, 9679-9684 (2009).
  5. Krzewska, J., Tanaka, M., Burston, SG., and Melki, R.:
    "Biochemical and functional analysis of the assembly of full-length Sup35p and its prion-forming domain."
    J. Biol. Chem., 282, 1679-1686 (2007).
  6. Tanaka, M., Collins, SR., Toyama, BH., and Weissman, JS.:
    "The physical basis of how prion conformations determine strain phenotypes."
    Nature, 442, 585-589 (2006).
  7. Tanaka, M., Chien, P., Yonekura, K., and Weissman, JS.:
    "Mechanism of cross-species prion transmission: an infectious conformation compatible with two highly divergent yeast prion proteins."
    Cell, 121, 49-62 (2005).
  8. Tanaka, M., Chien, P., Naber, N., Cooke, R., and Weissman, JS.:
    "Conformational variations in an infectious protein determine prion strain differences."
    Nature, 428, 323-328 (2004).
  9. Venkatraman, P., Wetzel, R., Tanaka, M., Nukina, N., and Goldberg, AL.:
    "Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins."
    Mol. Cell, 14, 95-104 (2004).
  10. Tanaka, M., Machida, Y., Niu, S., Ikeda, T., Jana, NR., Doi, H., Kurosawa, M., Nekooki, M., and Nukina, N.:
    "Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease."
    Nature Med., 10, 148-154 (2004).
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