The mechanism of osmo-regulatory signal transduction by interactions among membrane proteins through their TM regions
| Project/Area Number |
24247034
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| Research Category |
Grant-in-Aid for Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Cell biology
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| Research Institution | The University of Tokyo |
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Principal Investigator |
SAITO Haruo 東京大学, 医科学研究所, 教授 (60114485)
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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 |
¥45,890,000 (Direct Cost: ¥35,300,000、Indirect Cost: ¥10,590,000)
Fiscal Year 2014: ¥14,950,000 (Direct Cost: ¥11,500,000、Indirect Cost: ¥3,450,000)
Fiscal Year 2013: ¥14,560,000 (Direct Cost: ¥11,200,000、Indirect Cost: ¥3,360,000)
Fiscal Year 2012: ¥16,380,000 (Direct Cost: ¥12,600,000、Indirect Cost: ¥3,780,000)
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| Keywords | Signal transduction / Yeast / Osmoregulation / Membrane protein / MAP kinase / シグナル伝達 / 酵母 / 浸透圧応答 / 膜タンパク質 / MAPキナーゼ / ４回膜タンパク質 |
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| Outline of Final Research Achievements |
When exposed to hyperosmolarity, the budding yeast Saccharomyces cerevisiae activates the Hog1 MAP kinase signal pathway, which governs an array of adaptive responses. In this project, we investigated how the activity of the Hog1 MAPK pathway is regulated by the Sho1 osmosensor and the Hkr1/Msb2 co-osmosensors. First, we determined the oligomeric structure of the 4TM osmosensor Sho1 using a site-directed chemical crosslinking strategy. External osmolarity influenced the internal structure of the Sho1 oligomer as well as the interactions between the Sho1 oligomers and cytoplasmic signaling proteins. Second, we found that specific and dynamic bindings of the Hkr1/Msb2 co-osmosensors to the membrane anchorage protein Opy2 and to cytoplasmic scaffold proteins are essential for Hog1 activation. From these results, details of the mechanism of Hog1 activation by external high osmolarity are revealed.
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Report
(4 results)
Research Products
(10 results)
