Functional regulation of proteins by Cys phosphorylation
| Project/Area Number |
16K14723
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Cell biology
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| Research Institution | Osaka University |
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Principal Investigator |
Miki Hiroaki 大阪大学, 微生物病研究所, 教授 (80302602)
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| Project Period (FY) |
2016-04-01 – 2020-03-31
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| Project Status |
Completed (Fiscal Year 2019)
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| Budget Amount *help |
¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2018: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2017: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2016: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
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| Keywords | 蛋白質 / シグナル伝達 / ストレス / 癌 |
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| Outline of Final Research Achievements |
We investigated the phosphorylation that occurs on Cys residue in oncogenic protein PRL. When magnesium ion was depleted from the culture medium, PRL was rapidly dephosphorylated and its protein levels were increased. PRL knockdown under this magnesium ion-depleted condition resulted in promotion of cell death, indicating the biological importance of this response. Moreover, the investigation of the phosphorylation mechanism revealed the possible role of phosphate-containing molecules, such as ATP, as phosphate donor.
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| Academic Significance and Societal Importance of the Research Achievements |
リン酸化はタンパク質の主要な翻訳後修飾として知られるが、システイン残基のリン酸化はこれまでにバクテリアでの事例が一つしか知られていないユニークなものである。本研究では発がん因子PRLでのシステインリン酸化に関する解析を進め、細胞の環境応答の仕組みとしてダイナミックに制御されており、それが細胞の生死に関わることを明らかにした。タンパク質機能制御の新たな仕組みとして今後の研究の発展が期待できる。
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Report
(5 results)
Research Products
(59 results)
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[Journal Article] Control of Protein Function Through Oxidation and Reduction of Persulfidated States2020
Author(s)
E Doka, T Ida, M Dagnell, Y Abiko, N C Luong, N Balog, T Takata, B Espinosa, A Nishimura, Q Cheng, Y Funato, H Miki, J M Fukuto, J R Prigge, E E Schmidt, E S J Arner, Y Kumagai, T Akaike, P Nagy
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Journal Title
Sci Adv
Volume: 6
Issue: 1
Pages: 8358-8358
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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