Unraveling of mechanisms of raft signaling as revealed by single-molecule imaging at high resolution
| Project/Area Number |
24370055
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | Kyoto University |
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Principal Investigator |
SUZUKI Kenichi 京都大学, 物質-細胞統合システム拠点, 准教授 (50423059)
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| Co-Investigator(Renkei-kenkyūsha) |
ANDO Hiromune 岐阜大学, 応用生物科学部, 准教授 (20372518)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥19,110,000 (Direct Cost: ¥14,700,000、Indirect Cost: ¥4,410,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2013: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2012: ¥15,860,000 (Direct Cost: ¥12,200,000、Indirect Cost: ¥3,660,000)
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| Keywords | 細胞情報伝達機構 / 細胞膜ドメイン / ラフト / 1分子観察 / 脂質ラフト / １分子観察 |
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| Outline of Final Research Achievements |
The purpose of this study is to unravel the regulation mechanisms of signal transduction in lipid rafts of cell plasma membranes. We tracked single molecules of representative raft molecules, GPI-anchored proteins and gangliosides in living cell membranes. Surprisingly, these raft markers formed transient homodimers which were stabilized by cholesterol. In general, the lifetime of the heterodimers were shorter than those of the homodimers. Our results suggest that these homodimers are induced by spesific protein interactions or specific sugar-chain interactions. Based on these results, we proposed a hypothesis that these homodimers are basic units for creating greater raft domains.
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Report
(4 results)
Research Products
(32 results)
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[Journal Article] Archipelago architecture of the focal adhesion: Membrane molecules freely enter and exit from the focal adhesion zone2012
Author(s)
A. C. E. Shibata, T. K. Fujiwara, L. Chen, K. G. N. Suzuki, Y. Ishikaia, Y. L. Nemoto, Y. Miwa, Z. Kalay, R. Chadda, K. Naruse, and A. Kusumi
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Journal Title
Cytoskeleton
Volume: 69
Issue: 6
Pages: 380-392
DOI
Related Report
Peer Reviewed
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[Presentation] Single-molecule tracking of new ganglioside probes revealed raft organization and function2013
Author(s)
Suzuki, K. G. N., Ando, H., Komura, N., Chadda, R., Ishida, H., Kiso, M., Kusumi, A.
Organizer
日本生物物理学会
Place of Presentation
京都国際会館
Related Report
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