Our goal is to elucidate molecular mechanisms of protein aggregation and its physiological consequences in neuropsychiatric diseases.

Motomasa TanakaMotomasa Tanaka

Motomasa Tanaka, Ph.D.

Team Leader, Protein Conformation Diseases
motomasa.tanaka [at] riken.jp

Research Overview

We are investigating the molecular basis of neuropsychiatric diseases using both in vivo and in vitro systems with a variety of techniques including neuroscience, genetics, chemical biology and structural biology. In conjunction, we are seeking to develop novel proteomics or genomics technologies to advance our understanding of the mechanisms of cellular aging and abnormal mRNA translation. Furthermore, we will uncover the structural basis of formation, disaggregation and propagation of amyloid fibers using the yeast prion system that we have established.

Main Research Field

Related Research Fields


Selected Publications

  1. Endo R., Takashima N., Nekooki-Machida Y., Komi Y., Hui K.K., Takao M., Akatsu H., Murayama S., Sawa A., and Tanaka M.: TDP-43 and DISC1 Co-Aggregation Disrupts Dendritic Local Translation and Mental Function in FTLD. Biol. Psychiatry, 84, 509-521 (2018).
  2. Chen  C.W., Tanaka M. Genome-Wide Translation Profiling by Ribosome-Bound tRNA Capture. Cell Rep., 23, 608-621 (2018).
  3. Ohhashi Y., Yamaguchi Y., Kurahashi H., Kamatari Y.O., Sugiyama S., Uluca B., Piechatzek T., Komi Y., Shida T., Müller H., Hanashima S., Heise H., Kuwata K, and Tanaka M. Molecular basis for diversification of yeast prion strain conformation, Proc. Natl. Acad. Sci. U. S. A., 115, 2389-2394 (2018).
  4. Tanaka, M., Ishizuka, K., Nekooki-Machida, Y., Endo, R., Takashima, N., Sasaki, H., Komi, Y., Gathercole, A., Huston, E., Ishii, K., Hui, K.K., Kurosawa, M., Kim, S.H., Nukina, N.,Takimoto, E., Houslay, M.D., and Sawa, A.:
    "Aggregation of scaffolding protein DISC1 dysregulates phosphodiesterase 4 in Huntington's disease."
    J. Clin. Invest., 127, 1438-1450 (2017).
  5. Suzuki, G., Weissman, J.S., and Tanaka, M.:
    "[KIL-d] protein element confers antiviral activity via catastrophic viral mutagenesis."
    Mol. Cell, 60, 651-660 (2015).
  6. Tanaka, M. and Komi, Y.:
    "Layers of structure and function in protein aggregation."
    Nat. Chem. Biol., 11, 373-377 (2015).
  7. Suzuki, G., Shimazu, N., and Tanaka, M.:
    "A Yeast Prion, Mod 5, Promotes Acquired Drug Resistance and Cell Survival Under Environmental Stress."
    Science 336, 355-359 (2012).
  8. Ohhashi, Y., Ito, K., Toyama, B.H., Weissman, J.S., and Tanaka, M.:
    "Differences in prion strain conformations result from non-native interactions in a nucleus."
    Nat. Chem. Biol. 6, 225-230 (2010).
  9. Nekooki-Machida, 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, 9678-9684(2009).
  10. Tanaka, M., Collins, S.R., Toyama, B.H., and Weissman, J.S.:
    "The Physical Basis of How Prion Conformations Determine Strain Phenotypes."
    Nature, 442, 585-589 (2006).