Analysis of the mechanism of the degradation of aggregation prone proteiins by a novel ubiquitin binding protein CG5445
| Project/Area Number |
16K08228
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Biological pharmacy
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| Research Institution | The University of Tokyo |
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Principal Investigator |
Hamazaki Jun 東京大学, 大学院薬学系研究科(薬学部), 助教 (80533588)
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| Project Period (FY) |
2016-04-01 – 2019-03-31
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| Project Status |
Completed (Fiscal Year 2018)
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| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2018: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
Fiscal Year 2017: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2016: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
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| Keywords | プロテアソーム / ユビキチン / タンパク質分解 / 分子生物学 / 神経変性疾患 |
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| Outline of Final Research Achievements |
Ubiquitin-proteasome system (UPS) plays essential role in eukaryotes. Since ubiquitin including aggregates are observed in neurodegenerative diseases, disruption of UPS are considered to participate in pathogenic mechanism. We identified CG545 as a novel ubiquitin binding protein. We clarify CG5445 plays a role in degradation of ubiquitinated aggregation-prone proteins to decrease their cytotoxicity until they are degraded.
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| Academic Significance and Societal Importance of the Research Achievements |
生体内における不要タンパク質除去に働く分解系のうち、ユビキチン-プロテアソーム系が凝集性タンパク質の分解にどのように働くかについては長い間様々な仮説が提唱されているものの、実態は不明であった。本課題において易凝集性タンパク質分解においてプロテアソーム機能を促進する分子としてCG5445を同定したことにより、プロテアソームが神経変性疾患をはじめとする病態発症に関与する分子機構の解明に大きな進歩をもたらすと考えられる。
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Report
(4 results)
Research Products
(37 results)
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[Journal Article] Specific modification of aged proteasomes revealed by tag-exchangeable knock-in mice.2018
Author(s)
Tomita, T., Hirayama, S., Sakurai, Y., Ohte, Y., Yoshihara, H., Saeki, Y., Hamazaki, J., and Murata, S.
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Journal Title
Mol. Cell Biol.
Volume: 39
Issue: 1
DOI
Related Report
Peer Reviewed / Open Access
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[Journal Article] Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets.2017
Author(s)
Lu X, Nowicka U, Sridharan V, Liu F, Ramdles L, Hymel D, Dyba M, Tarasov SG, Tarasova NI, Zhao XZ, Hamazaki J, Murata S, Burke TR Jr, Walters KJ.
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Journal Title
nature communications
Volume: 8
Issue: 1
Pages: 15540-15540
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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[Journal Article] Foxn1-β5t transcriptional axis controls CD8+ T cell production in the thymus.2017
Author(s)
Uddin MM, Ohigashi I, Motosugi R, Nakayama T, Sakata M, Hamazaki J, Nishito Y, Rode I, Tanaka K, Takemoto T, Murata S, Takahama Y.
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Journal Title
Nat Commun
Volume: 8
Issue: 1
Pages: 14419-14419
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research / Acknowledgement Compliant
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