PRIP mediates autophagic elimination of intracellular bacteria.
| Project/Area Number |
25861757
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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 |
Functional basic dentistry
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| Research Institution | Hiroshima University |
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Principal Investigator |
HARADA Kae 広島大学, 医歯薬保健学研究院(歯), 助教 (60432663)
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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 |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2014: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2013: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | オートファジー / 細菌感染 / 微生物 |
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| Outline of Final Research Achievements |
PRIP (PLC-related catalytically inactive protein) interacts with both LC3 and GABARAP which are modulators of autophagy. We previously reported that PRIP regulates autophagic pathway triggered by amino-acid starvation.
In this study, we explored autophagic pathway in PRIP-deficient (Prip-DKO) cells infected with Staphylococcus aureus. LC3-positive autophagosome-like vacuoles (SAcAVs) in Prip-DKO cells enclosed more S. aureus than wild-type cells, suggesting that S. aureus proliferates in the SAcAVs of Prip-DKO cells. Then, autophagic flux was analyzed using an RFP-GFP-tagged LC3 and a lysosomal dye. Autophagosome maturation, the fusion between autophagosome and lysosome, was significantly inhibited in Prip-DKO cells.
These data indicate that PRIP mediates the fusion of SAcAVs with lysosomes and is a novel autophagy modulator which combats infection of pathogenic bacteria in host cells.
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Report
(3 results)
Research Products
(13 results)
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[Journal Article] Phospholipase C-Related Catalytically Inactive Protein (PRIP) regulates lipolysis in adipose tissue by modulating the phosphorylation of hormone-sensitive lipase2014
Author(s)
T. Okumura, K. Harada, K. Oue, J. Zhang, S. Asano, M. Hayashiuchi, A. Mizokami, H. Tanaka, M. Irifune, N. Kamata, M. Hirata, and T. Kanematsu.
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Journal Title
PLoS One
Volume: 9
Issue: 6
Pages: e100559-e100559
DOI
Related Report
Peer Reviewed / Open Access
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