Nuclear export mechanism of misfolded proteins
| Project/Area Number |
16K20998
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Cell biology
Functional biochemistry
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| Research Institution | The University of Tokyo |
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Principal Investigator |
Hirayama Shoshiro 東京大学, 大学院薬学系研究科(薬学部), 助教 (80548280)
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| Project Period (FY) |
2016-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2017: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2016: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | ユビキチン / プロテアソーム / タンパク質品質管理 / 細胞内輸送 / タンパク質凝集体 / 神経変性疾患 / タンパク質凝集 / 細胞生物学 / 蛋白質品質管理 |
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| Outline of Final Research Achievements |
In mammalian cells, it is known that the misfolded or the ubiquitinated proteins are sequestered into specific deposition sites in the cytoplasm not in the nucleus such as aggresome and ALIS. Formation of these cytoplasmic aggregates is considered to be cytoprotective. However, it is unknown why aggresome and ALIS form in the cytosol but not in the nucleus.
In this study, we found that the ubiquitinated proteins were exported from the nucleus and cytosol. Furthermore, we also showed that ubiquitin binding protein UBIN and its cofactor POST cooperatively export the ubiquitinated proteins in an exportin dependent manner.
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Report
(3 results)
Research Products
(11 results)
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[Journal Article] A small-molecule compound inhibits a collagen-specific molecular chaperone and could represent a potential remedy for fibrosis2017
Author(s)
S. Ito, K. Ogawa, K. Takeuchi, M. Takagi, M. Yoshida, T. Hirokawa, S. Hirayama, K. Shin-Ya, I. Shimada, T. Doi, N. Goshima, T. Natsume, K. Nagata
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Journal Title
J. Biol. Chem.
Volume: 292
Issue: 49
Pages: 20076-20085
DOI
Related Report
Peer Reviewed / Open Access
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