Determination of aPKC substrates in the regulation of cell polarity.
| Project/Area Number |
13670129
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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 medical chemistry
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| Research Institution | Yokohama City University |
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Principal Investigator |
MIZUNO Keiko Yokohama City Univ., Sch.of Medicine, assistant instructor, 医学部, 助手 (90221803)
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| Project Period (FY) |
2001 – 2003
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| Project Status |
Completed (Fiscal Year 2003)
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| Budget Amount *help |
¥1,800,000 (Direct Cost: ¥1,800,000)
Fiscal Year 2003: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 2002: ¥900,000 (Direct Cost: ¥900,000)
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| Keywords | Cell polarity / atypical PKC / PAR-3 / ASIP |
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| Research Abstract |
Atypical protein kinase C (aPKC)-PAR complex is evolutionary conserved proteins and play essential roles on the establishment of cell polarity. In mammalian epithelial cells, aPKC co-localizes with PAR-3/ASIP and PAR-6 to the tight junction (TJ) and is essential for the establishment of TJ, although molecular mechanism regulating cell polarity remains unknown. One of the aPKC-binding proteins, 14-3-3/PAR-5 has been reported to be involved in the regulation of cell polarity in C. elegance embryo or Drosophila. In this study, I demonstrated that mammalian PAR-3 could bind to 14-3-3 in phosphorylation dependent manner. I also determined the Ser rsidue of PAR-3 subject to specific antibody demonstrated the phosphorylation of this Ser residue in polarized MDCK cells. In residue of GST-PAR-3 as substrate. These results suggest that aPKC phosphorylates this Ser on PAR-3 and regulates the binding of PAR-3 and 14-3-3/PAR-5.
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Report
(4 results)
Research Products
(19 results)
