Focused proteomics of phosphorylated proteins using tautomycetin and its application
Project/Area Number |
19208011
|
Research Category |
Grant-in-Aid for Scientific Research (A)
|
Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Bioproduction chemistry/Bioorganic chemistry
|
Research Institution | Hokkaido University |
Principal Investigator |
UBUKATA Makoto Hokkaido University, 大学院・農学研究院, 教授 (60168739)
|
Co-Investigator(Renkei-kenkyūsha) |
MITSUHASHI Shinya 北海道大学, 大学院・農学研究院, 学術研究員 (60526672)
|
Research Collaborator |
SHIGETOMI Kenngo 北海道大学, 大学院・農学研究院, 学術研究員 (20547202)
|
Project Period (FY) |
2007 – 2009
|
Project Status |
Completed (Fiscal Year 2009)
|
Budget Amount *help |
¥27,820,000 (Direct Cost: ¥21,400,000、Indirect Cost: ¥6,420,000)
Fiscal Year 2009: ¥7,020,000 (Direct Cost: ¥5,400,000、Indirect Cost: ¥1,620,000)
Fiscal Year 2008: ¥7,410,000 (Direct Cost: ¥5,700,000、Indirect Cost: ¥1,710,000)
Fiscal Year 2007: ¥13,390,000 (Direct Cost: ¥10,300,000、Indirect Cost: ¥3,090,000)
|
Keywords | PP1 / TNFα / NF-κB / IKK / RPS3a / トウトマイセチン / 1型ホスファターゼ / 阻害剤 / リン酸化 / ATM / MF-κB |
Research Abstract |
We have conducted focused proteomics of phosphorylated proteins by using tautomycetin. Protein phosphatase 1 (PP1) was found to act as a kind of regulatory enzyme for signal transduction in mammalian cells. For example, it positively regulates TNFα/NF-κB pathway as well as Raf. In addition, we isolated ATM30, a substrate of both PP1 and ATM/ATR kinase. ATM30 was found to be a ribosomal protein RPS3A(a) by MALDI-TOF/MS analysis.
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Report
(4 results)
Research Products
(50 results)