| Project/Area Number |
18570186
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Cell biology
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| Research Institution | Tokyo University of Pharmacy and Life Science |
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Principal Investigator |
TANI Katsuko Tokyo University of Pharmacy and Life Science, School of Life Sciences, Associate Professor (40266896)
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| Co-Investigator(Kenkyū-buntansha) |
NAGISA Arimitsu Tokyo University of Pharmacy and Life Sciences, School of Life Sciences, Research Associate (40408688)
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| Project Period (FY) |
2006 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥4,110,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥510,000)
Fiscal Year 2007: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Fiscal Year 2006: ¥1,900,000 (Direct Cost: ¥1,900,000)
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| Keywords | Phospholipid / Membrane traffic / Oreanelle / Phosphatidic acid / Phospholipase |
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| Research Abstract |
The mammalian intracellular phospholipase A1 family consists of three members, phosphatidic acid-preferring phospholipase A1 (PA-PLA1), p125, and KIAA0725p. In a previous study, we showed that p125 is a mammalian-specific component of ER exit sites and participates in the organization of this compartment. In this study, we examined the function of KIAA0725p. In addition, the binding affinity of three proteins to various phospholipids was analyzed.
1) To gain insight into the function of KIAA0725p, KIAA0725p mRNA was targeted for degradation by RNAi. In KIAA0725p-depleted cells, the organization of the Golgi apparatus was subtly affected. VSV-G Protein transport from the Golgi to plasma membrane and Shiga-toxin transport from the plasma membrane to the Golgi were affected in these cells. These results suggest that KIAA0725p participates in protein transport between the Golgi and the plasma membrane.
2) Recombinant proteins were purified from Sf9 cells and used to analyze their binding to various phoispholipids. We found that p125 and KIAA0725p bind to phosphatidylinositol 3-phosphate (PI3P), PI4P, and PI5P. On the other hand, PA-PLA1 did not bind to any lipids under the same condition. KIAA0725p and PA-PLA1localize to the Golgi apparatus and the cytosol, respectively. These results rise the possibility that PIP is a membrane receptor for p125 and KIAA0725p.
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