Laboratory for Protein Conformation Diseases

Laboratory Head
Motomasa TANAKA (Ph.D.)
We investigate molecular basis of neurodegenerative disorders and psychiatric diseases by using a variety of methods including neurobiology, genetics, structural biology and proteomics. Furthermore, we aim to reveal structural basis of prion strains and transmission barriers in yeast prion systems by various biophysical techniques and yeast genetics. We also search for and analyze novel cytoplasmic genetic elements and functional amyloids that play physiological roles in cells.
- Protein misfolding and neurodegenerative diseases
- Molecular basis of mental disorders
- Identification and analysis of novel functional amyloid
- Structural basis of yeast prion strains and transmission barriers
- 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.
- Suzuki, G., Shimazu, N., and Tanaka, M.:
"A Yeast Prion, Mod 5, Promotes Acquired Drug Resistance for Cell Survival under Environmental Stress"
Science, in press (2012) - Tanaka, M.:
" Protein misfolding: tracking a toxic polyglutamine epitope"
Nat. Chem. Biol., 7, 861-862 (2011). - Tonoki A, Kuranaga E, Ito N, Nekooki-Machida Y, Tanaka M, and Miura M:
" Aging causes distinct characteristics of polyglutamine amyloids in vivo"
Genes Cells, 16, 557-64 (2011). - Foo CK, Ohhashi Y, Kelly MJ, Tanaka M, and Weissman JS:
" Radically different amyloid conformations dictate the seeding specificity of a chimeric Sup35 prion"
J. Mol. Biol., 408, 1-8 (2011) - Ohhashi, Y., Ito, K., Toyama, GH, Weissman, JS., and Tanaka, M.:
" Differences in prion strain conformations result from non-native interactions in a nucles"
Nat. Chem. Biol., 6, 225-230 (2010). - 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, 9679-9684 (2009). - 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). - Tanaka, M., Collins, SR., Toyama, BH., and Weissman, JS.:
" The physical basis of how prion conformations determine strain phenotypes"
Nature, 442, 585-589 (2006). - 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). - 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"
Nat. Med., 10, 148-154 (2004).
Principal Investigator
- Motomasa TANAKA
- Laboratory Head
Members
- Yusuke KOMI
- Research Scientist
- Genjiro SUZUKI
- Research Scientist
- Yumiko OHHASHI
- Research Scientist
- Ryo ENDO
- Research Scientist
- Chien-Wen CHEN
- Research Scientist
- Kai-Wan Kelvin HUI
- Visiting Researcher
- Hiroki YOSHISE
- Student Trainee
- Yoko NEKOOKI
- Technical Staff I
- Mao YAMAGUCHI
- Technical Staff I
- Miwa HIGAKI
- Part-time Staff
- Naomi TAKAHASHI
- Part-time Staff
- Mizue HONDA
- Part-time Staff