2011 Fiscal Year Final Research Report
Quality control mechanism of misfolded proteins
| Project/Area Number |
19GS0314
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| Research Category |
Grant-in-Aid for Creative Scientific Research
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| Allocation Type | Single-year Grants |
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| Research Institution | Kyoto Sangyo University (2011)
Kyoto University (2007-2010) |
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Principal Investigator |
NAGATA Kazuhiro 京都産業大学, 総合生命科学部, 教授 (50127114)
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| Co-Investigator(Kenkyū-buntansha) |
INABA Kenji 九州大学, 生体防御医学研究所, 准教授 (10423039)
HOSOKAWA Nobuko 京都大学, 再生医科学研究所, 准教授 (00263153)
HOSEKI Jun 京都大学, 生理化学研究ユニット, 特定准教授 (40423058)
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| Project Period (FY) |
2007 – 2011
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| Keywords | 品質管理 / フォールディング / レドックス / 小胞体 |
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| Research Abstract |
Our study was performed by focusing two issues in protein quality control in the endoplasmic reticulum (ER). The first one was on the productive folding of nascent polypeptides by molecular chaperones and oxidoredcutases in the ER. The second one was to reveal the quality control mechanism of ER-associated degradation (ERAD) system that eliminates the misfolded proteins from the ER. We found two novel factors involved in the ERAD, EDEM1 and ERdj5. In this term, mainly three issues on this proposal was addressed: 1) we succeeded to solve the crystal structure of ERdj5 that reduces the disulfide bonds in the misfolded proteins to be degraded and proposed the substrate transfer pathway in the ERAD system for glycoproteins, 2) we revealed the novel ERAD pathway for misfolded non-glycosylated proteins, and 3) we showed the electron transfer pathway in the process of oxidation including Ero1a, PDI and ERp46.
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Research Products
(38 results)
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[Journal Article] A pH-Regulated Quality Control Cycle forSurveillance of Secretory Protein Assembly2013
Author(s)
S.Vavassori, M. Cortini, S. Masui, S.Sannino,T.Anelli, I. R.Caserta, C.Fagioli, A.Fornili, M.F.Mossuto, M .Degano, K.Inaba, & R.Sitia
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Journal Title
Molecular Cell
Volume: (in press)
Peer Reviewed
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[Journal Article] The mutation incyclophilin B that causes hyperelastosis cutis in the American Quarter Horse does not affectpeptidyl-prolyl cis-trans isomerase activity, butshows altered cyclophilin B-protein interactionsand affects collagen folding2012
Author(s)
Y. Ishikawa, J. A. Vranka, S. P. Boudko, E.Pokidysheva, K. Mizuno, K. Zientek, D. R.Keene, A. M. Rashmir-Raven, K. Nagata, N. J.Winand and H. P. Bachinger
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Journal Title
J. Biol. Chem
Volume: 287(26)
Pages: 22253-22265
DOI
Peer Reviewed
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[Journal Article] Dynamicnature of disulfide bond formation catalystsrevealed by crystal structures of DsbB2009
Author(s)
Inaba, K., Murakami, S., Nakagawa, A., Iida,H., Kinjo, M., Ito, K. and Suzuki, M.
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Journal Title
EMBO J
Volume: 28
Pages: 779-791
DOI
Peer Reviewed
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[Journal Article] A pair of circularlypermutated PDZ domains control RseP, the S2Pfamily intramembrane protease of E. coli2008
Author(s)
Inaba, K., Suzuki, M., Maegawa, K., Akiyama,S., Ito, K. and Akiyama, Y.
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Journal Title
J. Biol. Chem.
Volume: 283
Pages: 35042-52
DOI
Peer Reviewed
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