Osmosensing mechanisms via oligomerization and dynamic interactions of the membrane proteins
Project/Area Number |
24370053
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Partial Multi-year Fund |
Section | 一般 |
Research Field |
Functional biochemistry
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Research Institution | The University of Tokyo |
Principal Investigator |
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Project Period (FY) |
2012-04-01 – 2016-03-31
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Project Status |
Completed (Fiscal Year 2015)
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Budget Amount *help |
¥18,200,000 (Direct Cost: ¥14,000,000、Indirect Cost: ¥4,200,000)
Fiscal Year 2014: ¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2013: ¥5,850,000 (Direct Cost: ¥4,500,000、Indirect Cost: ¥1,350,000)
Fiscal Year 2012: ¥7,020,000 (Direct Cost: ¥5,400,000、Indirect Cost: ¥1,620,000)
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Keywords | 高浸透圧 / センサー / 酵母 / HOG経路 / 膜タンパク質 / 多量体 / 結合 / 結合ドメイン / 浸透圧 / MAPキナーゼ / 膜蛋白質 / クロスリンク / 高浸透 |
Outline of Final Research Achievements |
In this study, I identified the four-transmembrane domain protein Sho1 as an osmosensor in the SHO1 branch of the yeast osmoreguratory HOG pathway. Structural changes are induced in the transmembrane regions of Sho1 by high osmolarity, leading to the increased binding of Sho1 to the cytoplasmic adaptor Ste50, accompanied by Hog1 activation. Chemical cross-linking analyses revealed that Sho1 forms homo oligomer of the dimers-of-trimers architectures by dimerizing at the TM1/4 interface and trimerizing at the TM2/3 interface. In addition, the TM1/4 interface of Sho1 binds to the membrane anchor Opy2, while the TM2/3 interface binds to the osmosensor Hkr1, indicating that Sho1 serves not only as an osmosensor but also as a scaffold.
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Report
(5 results)
Research Products
(15 results)
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[Journal Article] Scaffold Protein Ahk1, Which Associates with Hkr1, Sho1, Ste11, and Pbs2, Inhibits Cross Talk Signaling from the Hkr1 Osmosensor to the Kss1 Mitogen-Activated Protein Kinase.2016
Author(s)
Nishimura A, Yamamoto K, Oyama M, Kozuka-Hata H, Saito H, Tatebayashi K.
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Journal Title
Mol Cell Biol
Volume: 36
Issue: 7
Pages: 1109-1123
DOI
Related Report
Peer Reviewed
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