| Project/Area Number |
26292188
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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 |
Applied molecular and cellular biology
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| Research Institution | Hokkaido University |
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Principal Investigator |
YAMAGUCHI Junji 北海道大学, 理学(系)研究科(研究院), 教授 (10183120)
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| Co-Investigator(Kenkyū-buntansha) |
佐藤 長緒 北海道大学, 理学(系)研究科(研究院), 助教 (50609724)
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| Co-Investigator(Renkei-kenkyūsha) |
SAKO Kaori 独立行政法人理化学研究所, 環境資源科学研究センター, 研究員 (60722395)
MAEKAWA Shugo 東京大学, 大学院農学生命科学研究科（農学部）, 特別研究員 (80711209)
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥17,940,000 (Direct Cost: ¥13,800,000、Indirect Cost: ¥4,140,000)
Fiscal Year 2016: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2015: ¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2014: ¥11,180,000 (Direct Cost: ¥8,600,000、Indirect Cost: ¥2,580,000)
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| Keywords | ユビキチンリガーゼ / 栄養学 / 膜交通 / 蛋白質 / 植物 |
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| Outline of Final Research Achievements |
Arabidopsis ATL31 is a membrane-localized ubiquitin ligase that functions in not only C/N-nutrient response but defense response. We identified SYP121 as a novel ATL31 interactor. SYP121 is an essential factor for plant resistance against powdery mildew fungus and positively regulates the formation of cell wall apposition, called papillae, at the fungal entry site. We finally indicated that ATL31 plays an important role in basal immunity by papilla formation through association with SYP121. The molecular basis of C/N-nutrient signaling also remains unclear. We identified three calcineurin B-like (CBL)-interacting protein kinases (CIPKs) as key regulators of the C/N-nutrient response. Further analyses showed that these CIPKs are required for ATL31 phosphorylation and stabilization, which mediates the degradation of 14-3-3 in response to C/N conditions in Arabidopsis. These findings provide new insights into C/N-nutrient signaling mediated by protein phosphorylation.
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