2002 Fiscal Year Final Research Report Summary
Regulatory mechanisms of CIC chloride channels by protein-protein interaction
| Project/Area Number |
13670035
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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 |
General physiology
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| Research Institution | Akita University |
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Principal Investigator |
FURUKAWA Tetsushi Akita University School of Medicine, Associate Professor, 医学部, 助教授 (80251552)
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| Project Period (FY) |
2001 – 2002
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| Keywords | chloride channel / protein-protein interaction / yeast two-hybrid system / cell cycle / cyclin-dependent kinase / ubiquitin / CFTR / PDZ domain |
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| Research Abstract |
(1) The C-terminus of ClC-2 channel is directly phosphorylated by M phase-specific cyclin-dependent kinase, p34^<cdc2>/cyclin B, and de-phosphorylated by protein phosphatase 1, for which protein-protein interaction plays a crucial role. ClC-2 channel expressed in Xenopus oocytes is inhibited by phosphorylation and activated by dephosphorylation.
(2) Western blot analysis and immunocytochemistry revealed that ClC-2 channel protein is expressed in dividing cells of the M phase of cell cycle, and promptly disappears after cell division. The PEST sequence is a signature of short-lived proteins via ubiquitination, and multiple PEST sequences are present in the C-terminus of ClC-2. Phosphorylation of ^<632>Ser of ClC-2 by p34^<cdc2>/cyclin B triggers ClC-2 channel ubiquitination, which underlines M phase-specific ubiquitination and degradation of ClC-2 channel protein.
(3) ClC-3B is a chloride channel expressed predominantly in epithelial cells and is localized in its microvilli. ClC-3B interacts With EBP50, an epithelia-specific PDZ-containing protein, and thereby interacts with cystic fibrosis transmembrane conductance regulator (CFTR), a product of cystic fibrosis gene. ClC-3B chloride channel is activated by protein kinase A in the presence of CFTR, and is important in ionic transport across the epithelia.
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Research Products
(12 results)
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[Publications] Furukawa, T., Ogura, T., Zheng, Y.-J., Tsuchiya, H., Nakaya., H., Katayama, Y., Inagaki, N.: "Phosphorylation and functional regulation of ClC-2 chloride channels expressed in Xenopus oocytes by M cyclin-dependent protein kinase"Journal of Physiology (London). 540. 883-893 (2002)
Description
「研究成果報告書概要(和文)」より
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[Publications] Ogura, T., Furukawa, T., Toyozaki, T., Yamada, K., Zheng, Y.-J., Katayama, Y, Nakaya.H., Inagaki, N.: "ClC-3B, a novel ClC-3 splicing variant that interacts with EBP50 and facilitates expression of CFTR-regulated ORCC"The FASEB Journal. 16. 863-865 (2002)
Description
「研究成果報告書概要(和文)」より
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[Publications] Furukawa, T., Ono, Y., Ysuchiya, H., Katayama, Y., Bang, M.-L., Labeit, D., Labeit, S., Inagaki, N., & Gregorio, C.C.: "Specific interaction of the potassium channel β-subunit minK with the sarcomeric protein T-cap suggests a T-tubule-myofibril linking system"Journal of Molecular Biology. 313. 775-784 (2001)
Description
「研究成果報告書概要(欧文)」より
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[Publications] Furukawa, T., Ogura, T., Zheng, Y.-J., Tsuchiya, H., Nakaya, H., Katayama, Y., & Inagaki, N.: "Phosphorylation and functional regulation of ClC-2 chloride channels expressed in Xenopus oocytes by M cyclin-dependent protein kinase"Journal of Physiology (London). 540. 883-893 (2003)
Description
「研究成果報告書概要(欧文)」より
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[Publications] Ogura, T., Furukawa, T., Toyozaki, T., Yamada, K., Zheng, Y.-J., Katayama, Y., Nakaya, H., & Inagaki, N.: "ClC-3B, a novel ClC-3 splicing variant that interacts with EBP50 and facilitates expression of CFTR-regulated ORCC."The FASEB Journal. 16. 863-865 (2002)
Description
「研究成果報告書概要(欧文)」より
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