The post-translational modification of NAD kinase governing the regulation of concentrations of cytosolic and mitochondrial NADP(H)
| Project/Area Number |
15K07387
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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 |
Applied biochemistry
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| Research Institution | Kyoto University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
村田 幸作 摂南大学, 理工学部, 教授 (90142299)
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2017: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2016: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2015: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
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| Keywords | NADキナーゼ / 翻訳後修飾 / NADP+ / NAD+ / フォスフォプロテオミクス解析 / Sirtuin / リン酸化 / 出芽酵母 |
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| Outline of Final Research Achievements |
The effect of phosphomimetic mutations at six of the phosphorylation sites (Ser residue) in human mitochondrial NAD kinase (mitNADK) were examined in vitro using the purified recombinant enzyme. The enzymatic activity was downregulated by a substitution of an Asp residue at Ser-289 and Ser-376, and completely inhibited by substituting Ser-188 with an Asp or Glu. Taken together that Ser-188 is highly conserved in the primary structures of mitNADK homologs in higher animals, this indicates that Ser-188 (and perhaps the other residues) is an important phosphorylation site that can downregulate the NAD kinase activity of this critical enzyme. However, it has remained still unclear how mitNADK and cytosolic NADK are regulated “in vivo” through phosphorylations in human and budding yeast cells.
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Report
(4 results)
Research Products
(10 results)
