PtdIns(3,4,5)P3 suppresses PTEN membrane binding in spontaneous formation of cellular polarity
| Project/Area Number |
25871120
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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 |
Biophysics
Cell biology
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| Research Institution | The Institute of Physical and Chemical Research |
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Principal Investigator |
MATSUOKA Satomi 独立行政法人理化学研究所, 生命システム研究センター, 研究員 (00569733)
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| Project Period (FY) |
2013-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2013: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | 細胞極性 / １分子イメージング / PTEN / PtdIns(3,4,5)P3 / 自己組織化 / 細胞性粘菌 / PI(3,4,5)P3 |
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| Outline of Final Research Achievements |
PtdIns(3,4,5)P3-enriched domain on cell membrane directs cell migration. I have examined single-molecule behaviors of 3-phosphatase, PTEN, in living Dictyostelium discoideum cells. PTEN undergoes transitions among 3 states with different lateral diffusivities. Enzymatically active state is the moderate one. Dephosphorylation accompanies prompt membrane dissociation. An amount of the active state depends on transition from the slowest state. PtdIns(3,4,5)P3 suppresses this state, finally reducing the PTEN amount on the membrane. Thus, PtdIns(3,4,5)P3 excludes PTEN from the membrane, illustrating that the positive feedback causes spontaneous formation of the domain in random cell migration.
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Report
(3 results)
Research Products
(13 results)
