2009 Fiscal Year Final Research Report
Molecular basis of polyglutamine disease using yeast
| Project/Area Number |
19680017
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| Research Category |
Grant-in-Aid for Young Scientists (A)
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| Allocation Type | Single-year Grants |
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| Research Field |
Neuroscience in general
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| Research Institution | The Institute of Physical and Chemical Research |
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Principal Investigator |
TANAKA Motomasa The Institute of Physical and Chemical Research, 田中研究ユニット, ユニットリーダー (40321781)
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| Project Period (FY) |
2007 – 2009
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| Keywords | ポリグルタミン / アミロイド / プリオン / 酵母 / 凝集体 |
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| Research Abstract |
We observed structural polymorphism in the aggregates of huntingtin, a protein responsible for Huntington disease, both in vitro and in vivo. Among distinct conformations of huntingtin amyloids derived from a variety of brain regions, those in striatum showed the highest cytotoxicity. Therefore, amyloid conformation may be a critical determinant of regional specificity in Huntington disease. In addition, a genetic screening system that can detect cross-seeding between a certain protein and polyglutamine aggregates allows us to identify a novel yeast prion protein that lacks a Gln/Asn-rich domain.
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[Journal Article] Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity.2009
Author(s)
Nekooki-Machida, Y., Kurosawa, M., Nukina, N., Ito, K., Oda, T., Tanaka, M.
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Journal Title
Proc. Natl. Acad. Sci. U.S.A. 106
Pages: 9679-9684
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