2003年8月
Self-association of PAR-3-mediated by the conserved N-terminal domain contributes to the development of epithelial tight junctions
JOURNAL OF BIOLOGICAL CHEMISTRY
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- 巻
- 278
- 号
- 33
- 開始ページ
- 31240
- 終了ページ
- 31250
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1074/jbc.M303593200
- 出版者・発行元
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
PAR-3 is a scaffold-like PDZ-containing protein that forms a complex with PAR-6 and atypical protein kinase C (PAR-3-atypical protein kinase C-PAR-6 complex) and contributes to the establishment of cell polarity in a wide variety of biological contexts. In mammalian epithelial cells, it localizes to tight junctions, the most apical end of epithelial cell-cell junctions, and contributes to the formation of functional tight junctions. However, the mechanism by which PAR-3 localizes to tight junctions and contributes to their formation remains to be clarified. Here we show that the N-terminal conserved region, CR1-(1-86), and the sequence 937-1,024 are required for its recruitment to the most apical side of the cell-cell contact region in epithelial Madin-Darby canine kidney cells. We also show that CR1 self-associates to form an oligomeric complex in vivo and in vitro. Further, overexpression of CR1 in Madin-Darby canine kidney cells disturbs the distribution of atypical protein kinase C and PAR-6 as well as PAR-3 and delays the formation of functional tight junctions. These results support the notion that the CR1- mediated self-association of the PAR-3-containing protein complex plays a role during the formation of functional tight junctions.
- リンク情報
- ID情報
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- DOI : 10.1074/jbc.M303593200
- ISSN : 0021-9258
- Web of Science ID : WOS:000184658800103