The role of PPP1r18, an actin binding protein, in osteoclastic bone resorption
Project/Area Number |
16K20423
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Functional basic dentistry
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Research Institution | Kyushu Dental College |
Principal Investigator |
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Co-Investigator(Renkei-kenkyūsha) |
JIMI Eijiro 九州歯科大学, 分子情報生化学分野, 教授 (40276598)
KOKABU Shoichiro 九州歯科大学, 分子情報生化学分野, 准教授 (30448899)
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Research Collaborator |
NAKATOMI Chihiro
URATA MARIKO
TOYAMA Kenya
KOBAYAKAWA Miki
YAGINUMA Tatsuki
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Project Period (FY) |
2016-04-01 – 2018-03-31
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Project Status |
Completed (Fiscal Year 2017)
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Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2017: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2016: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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Keywords | 破骨細胞 / 骨吸収 / Src / 骨代謝 / 細胞骨格 |
Outline of Final Research Achievements |
Osteoclasts in tyrosine kinase Src deficient mice that show osteopetrosis hardly resorb bone matrix because of disable to attachment to bone matrix. Src organizes actin accumulation and regulates actin ring formation for attachment. However molecular mechanisms how Src regulates actin ring formation in osteoclasts are not fully understood. We identified an actin binding protein PPP1r18 as Src binding protein by mass spectrum analysis. PPP1r18 was expressed and localized in actin ring with Src of osteoclasts. These results suggest that PPP1r18 bind to Src and involved in actin ring formation. Downregulation of PPP1r18 expression promoted actin ring formation. On the other hand, overexpression of PPP1r18 inhibited actin ring formation and bone resorption. Mutation of protein phosphatase 1 binding domain of PPP1r18 canceled inhibition of actin ring formation by PPP1r18. These results suggest that PPP1r18 negatively regulates actin ring formation and bone resorption.
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Report
(3 results)
Research Products
(33 results)
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[Journal Article] The transcriptional co-repressor TLE3 regulates myogenic differentiation by repressing the activity of the MyoD transcription factor.2018
Author(s)
Kokabu S, Nakatomi C, Matsubara T, Ono Y, Addison WN, Lowery JW, Urata M, Hudnall AM, Hitomi S, Nakatomi M, Sato T, Osawa K, Yoda T, Rosen V, Jimi E.
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Journal Title
Journal of Biological Chemistry.
Volume: 292
Issue: 31
Pages: 12885-12894
DOI
Related Report
Peer Reviewed / Open Access
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