1997 Fiscal Year Final Research Report Summary
Identification and characterization of CF kinase
Project/Area Number |
08458234
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Cell biology
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Research Institution | Aichi Cancer Center |
Principal Investigator |
INAGAKI Masaki Chief of Lab.of Biochemistry Aichi Cancer Cencer Research Institute, 生化学部, 部長 (30183007)
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Co-Investigator(Kenkyū-buntansha) |
INAGAKI Naoyuki Head of Lab.of Biochemistry Aichi Cancer Center Research Institute, 生化学部, 室長 (20223216)
|
Project Period (FY) |
1996 – 1997
|
Keywords | Intermediate filament / Cytokinesis / Rho-kinase / CF-kinase / Phosphorylation |
Research Abstract |
Cytokinesis is the mitotic precess in which all the essential cell components are segregated into postmitotic daughter cells It is suggested that protein phoshorylation plays pivotal roles in mitotic control, however the mechanisms for the cellular separation in cytokineses are not well characterized. We reported a protein kinase activity that phosphorylates a type III intermediate filament protein, glial fiberllary acidic protein (GFAP), specifically at the cleavage furrow of cytokinetic cells. It was termed cleavage furrow (CF) kinase. Now, we obtained evidence that Rho-associated Kinase (Rho-kinase) is a candidate for CF kinase ; Rho-kinase phosphorylated GFAP in vitro at the same sites that were phosphorylated by CF kinase in vivo. We also analyzed the functions of CF kinase/Rho-kinase activity by introducing mutant GFAPs into type III intermediate filament-negative cells. The mutation in CF kinase/Rho-kinase phosphorylation sites impaired GFAP segregation into postmitotic daughter cells. As a result, unusually long cytoplasmic bridge-like structure was formed between unseparated dughter cells. These results suggst that CF kinase/Rho-kinase is essential for the segragation of GFAP into daughter cells which in turn ensures efficient cellular separation.
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[Publications] Sekimata, M., Tsujimura, K., Tanaka, J., Takeuchi, Y., Inagaki, N., and Inagaki, M.: "Detection of protein kinase acitivity specifically activated at metaphase-anaphase transition." J.Cel Biol.132. 635-641 (1996)
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「研究成果報告書概要(欧文)」より
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[Publications] Takai, Y., Ogawara, M., Tomono, Y., Moritoh, C., Imajoh-Ohmi, S., Tsutsumi, O., Taketani, Y., and Inagaki, M.: "Mitosis-specific phosphorylation of vimentin by protein kinase C coupled with reorganizaition of intracellular membranes." J.Cel Biol.133. 141-149 (1996)
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[Publications] Inagaki, M., Matsuoka, Y., Tsujimura, K., Ando, S., Tokui, T., Takahashi, T., and Inagaki, N.: "Dynamic property of intermediate filaments : Regulation by phosphorylation." Bio Essays. 18. 481-487 (1996)
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[Publications] Kosako, H., Amano, M., Yanagida, M., Tanabe, K., Nishi, Y., Kaibuchi, K., and Inagaki, M.: "Phosphorylation of glial fibrillary acidic protein at the same sites by cleavage furrow kinase and Rho-associated kinase." J.Biol.Chem.272. 10333-10336 (1997)
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[Publications] Inagaki, N., Goto, H., Ogawara, M., Nishi, Y., Ando, S., and Inagaki, M.: "Spatial patterns of Ca^<2+> signals define the intracellular distribution of a signaling by Ca^<2+>/calmodulin-dependent protein kinase II." J.Biol.Chem.272. 25195-25199 (1997)
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