Mechanisms of cell cycle-dependent primary cilium formation and degradation
| Project/Area Number |
15H04347
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | Tohoku University |
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Principal Investigator |
Mizuno Kensaku 東北大学, 生命科学研究科, 教授 (70128396)
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥16,120,000 (Direct Cost: ¥12,400,000、Indirect Cost: ¥3,720,000)
Fiscal Year 2017: ¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2016: ¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2015: ¥5,980,000 (Direct Cost: ¥4,600,000、Indirect Cost: ¥1,380,000)
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| Keywords | 一次繊毛 / 細胞周期 / TTBK2 / NDR2 / アクチン / NDR / アクチンダイナミクス / TESK |
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| Outline of Final Research Achievements |
Primary cilia are antenna-like sensory organella that transmit various extracellular signals. Primary cilium formation is correlated with the exit from the cell cycle. In this project, we aimed to elucidate the mechanisms underlying cell-cycle-dependent primary cilium formation and obtained several findings as follows: 1) NDR2 localizes to peroxisomes in a manner dependent on the C-terminal GKL sequence, and this localization is required for its function in ciliogenesis. 2) The protein kinase activity of TTBK2 is promoted by the binding of the centrosomal protein Cep164. 3) Jasplakinolide, a potent inducer of actin polymerization, promotes ciliogenesis through cell rounding and YAP inactivation. 4) Glucose deprivation induces ciliogenesis through mTORC1 inactivation and p27KIP1 upregulation. 5) Cep97, a suppressor of primary cilium formation, is degraded upon serum starvation by the ubiquitin-proteasome system.
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Report
(4 results)
Research Products
(20 results)
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[Journal Article] Localization of protein kinase NDR2 to peroxisomes and its role in ciliogenesis.2017
Author(s)
Abe, S., Nagai, T., Masukawa, M., Okumoto, K., Homma, Y., Fujiki, Y., and Mizuno, K.
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Journal Title
J. Biol. Chem.
Volume: 292
Issue: 10
Pages: 4089-4098
DOI
Related Report
Peer Reviewed / Acknowledgement Compliant
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