Analysis of glycoprotein quality control in the secretory pathway of fission yeast cells
| Project/Area Number |
19380051
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Applied microbiology
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| Research Institution | Kyushu University (2008-2009)
Kagawa University (2007) |
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Principal Investigator |
TAKEGAWA Kaoru Kyushu University, 大学院・農学研究院, 教授 (50197282)
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| Co-Investigator(Kenkyū-buntansha) |
鈴木 匡 大阪大学, 医学研究科, 特任准教授 (90345265)
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| Co-Investigator(Renkei-kenkyūsha) |
SUZUKI Tadashi 理化学研究所, 基盤研究所・糖鎖代謝学チーム, チームリーダー (90345265)
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| Project Period (FY) |
2007 – 2009
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| Project Status |
Completed (Fiscal Year 2009)
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| Budget Amount *help |
¥19,760,000 (Direct Cost: ¥15,200,000、Indirect Cost: ¥4,560,000)
Fiscal Year 2009: ¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2008: ¥5,850,000 (Direct Cost: ¥4,500,000、Indirect Cost: ¥1,350,000)
Fiscal Year 2007: ¥8,970,000 (Direct Cost: ¥6,900,000、Indirect Cost: ¥2,070,000)
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| Keywords | 分裂酵母 / 糖タンパク質 / 異常タンパク質 / 品質管理機構 / 糖鎖付加 / タンパク分解 / N-結合型糖鎖 |
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| Research Abstract |
In both mammalian and yeast cells, proteins entering the secretory pathway adopt their final tertiary structure in the endoplasmic reticulum (ER). ER is the major organelle for folding of newly synthesized secretory proteins. A major regulator of this process is the quality control machinery, which retains and finally disposes of misfolded secretory proteins before they can exit the ER. The ER quality control process is highly conserved in eukaryotic cells, and are linked to a variety of diseases in mammalian cells. However, proteins required for the ER quality control system has not been analyzed and reported in the fission yeast Schizosaccharomyces pombe except UDP-glucose : glycoprotein glucosyltransferase. In this study, we studied proteins required for quality control mechanism of glycoprotein folding, and analyzed the glycosylation and processing of oligosaccharides in the ER in S. pombe cells.
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Report
(4 results)
Research Products
(48 results)
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[Journal Article] Tha och1 mutant of Schizosaccharomyces pombe produces galactosylated core structures of N-linked oligosaccharides.2009
Author(s)
Ohashi, T., Ikeda, Y., Tanaka, N., Nakakita, S., Natsuka, S., Giga-Hama, Y., Takegawa, K.
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Journal Title
Biosci. Biotechnol. Biochem. 73
Pages: 407-414
Related Report
Peer Reviewed
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[Journal Article] Production of heterologous proteins using the fission-yeast (Schizosaccharomyces pombe) expression system.2009
Author(s)
Takegawa, K., Tohda, H., Sasaki, M., Idiris, A., Ohashi, T., Mukaiyama, H., Giga-Hama, Y., Kumagai, H.
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Journal Title
Bioctechnol. Appl. Biochem. 53
Pages: 227-235
Related Report
Peer Reviewed
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[Journal Article] Production of heterologous proteins using the fission-yeast(Schizosaccharomyces pombe)expression system.2009
Author(s)
Takegawa, K., Tohda, H., Sasaki, M., Idiris, A., Ohashi, T., Mukaiyama, H., Giga-Hama, Y., Kumagai, H.
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Journal Title
Biotechnol.Appl.Biochem. 53
Pages: 227-235
Related Report
Peer Reviewed
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[Journal Article] The ochl mutant of Schizosaccharomyces pombe produces galactosylated core structures of N-linked oligosaccharides.2009
Author(s)
Ohashi, T., Ikeda, Y., Tanaka, N., Nakakita, S., Natsuka, S., Giga-Hama, Y., Takegawa, K.
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Journal Title
Bioscience, Biotechnology and Biochemistry 72
Pages: 407-414
Related Report
Peer Reviewed
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