Elucidation of the role of phospholipid metabolism in the prospore membrane formation of budding yeast
Project/Area Number |
25450094
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Applied microbiology
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Research Institution | The University of Tokyo |
Principal Investigator |
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Project Period (FY) |
2013-04-01 – 2016-03-31
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Project Status |
Completed (Fiscal Year 2015)
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Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2015: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2014: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2013: ¥2,990,000 (Direct Cost: ¥2,300,000、Indirect Cost: ¥690,000)
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Keywords | 生体膜 / リン脂質 / 微生物学 / 出芽酵母 / メンブレントラフィック / ジスフェリン / 胞子形成 |
Outline of Final Research Achievements |
Prospore membrane formation of Saccharomyces cerevisiae is a de novo membrane formation in side the cell to the proper size and proper shape and is a good model for membrane morphogenesis. We and other groups have been analyzing the genes involved in this process. Our genetic screen revealed that Phosphatidylinositol (PI) 4-kinase complex is involved in the prospore membrane formation. We also showed that PI4P and PI4-kinase complex together with Phosphatidic Acid and Phosphatidylserine are on the prospore membrane. Further, our analyses suggest that decrease of PI4P on the prospore membrane is related to extension of the prospore membrane, and that regulation of PI4P levels on the prospore membrane is important for its extension. Our result will contribute to the understanding of the role of PI4P in membrane formation in the cell.
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Report
(4 results)
Research Products
(15 results)
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[Journal Article] The Dysferlin domain-only protein, Spo73, is required for prospore membrane extension in Saccharomyces cerevisiae2016
Author(s)
Okumura Y, Nakamura TS, Tanaka T, Inoue I, Suda Y, Takahashi T, Nakanishi H, Nakamura S, Gao XD, Tachikawa H
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Journal Title
mSphere
Volume: 1
Issue: 1
Pages: 00038-15
DOI
NAID
Related Report
Peer Reviewed / Open Access / Int'l Joint Research / Acknowledgement Compliant
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