2015 Fiscal Year Final Research Report
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 |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | The University of Tokyo |
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Principal Investigator |
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| Project Period (FY) |
2012-04-01 – 2016-03-31
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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 |
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| 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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| Free Research Field |
分子生物学
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