Source:http://linkedlifedata.com/resource/pubmed/id/20859058
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2010-10-27
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pubmed:abstractText |
The role of p120-catenin in the function of classical cadherins is still enigmatic despite various studies. To elucidate its role, we examined the effect of p120-catenin on the N-cadherin-mediated localization of junctional proteins in epithelial cells in this study. Cadherin-deficient MIA PaCa-2 epithelial cells did not show linear localization of tight junction proteins ZO-1 and occludin. When N-cadherin was expressed in these cells, however, the resultant transfectant cells revealed strong cell adhesion activity and linear localization of ZO-1, occludin, and N-cadherin in the lateral membrane. When the p120-catenin-binding site of N-cadherin was disrupted, the linear localization of ZO-1 and occludin disappeared, and the mutant N-cadherin became localized more diffusely in the transfectant, although the cell adhesion activity did not change much. Knockdown of p120-catenin also resulted in the very weak localization of ZO-1 and occludin. A similar effect of p120-catenin on the localization of junctional proteins was obtained under more dynamic conditions in a wound healing assay. Moreover, p120-catenin was essential for the regulation of centrosome orientation in this healing assay. Taken together, the present data indicate that p120-catenin is essential for N-cadherin-mediated formation of proper junctional structures and thereby the establishment of the cell polarity. Similar results were obtained when E-cadherin mutants comparable to those of N-cadherin were used, suggesting that p120-catenin plays the same role in the function of other classical cadherins.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Catenins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/delta catenin,
http://linkedlifedata.com/resource/pubmed/chemical/occludin,
http://linkedlifedata.com/resource/pubmed/chemical/zonula occludens-1 protein
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pubmed:status |
MEDLINE
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pubmed:issn |
1347-3700
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
35
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
81-94
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pubmed:dateRevised |
2011-9-21
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pubmed:meshHeading |
pubmed-meshheading:20859058-Binding Sites,
pubmed-meshheading:20859058-Cadherins,
pubmed-meshheading:20859058-Catenins,
pubmed-meshheading:20859058-Cell Adhesion,
pubmed-meshheading:20859058-Cell Line, Tumor,
pubmed-meshheading:20859058-Cell Polarity,
pubmed-meshheading:20859058-Epithelial Cells,
pubmed-meshheading:20859058-Humans,
pubmed-meshheading:20859058-Immunoprecipitation,
pubmed-meshheading:20859058-Intercellular Junctions,
pubmed-meshheading:20859058-Membrane Proteins,
pubmed-meshheading:20859058-Phosphoproteins,
pubmed-meshheading:20859058-Protein Binding,
pubmed-meshheading:20859058-RNA, Small Interfering,
pubmed-meshheading:20859058-RNA Interference
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pubmed:year |
2010
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pubmed:articleTitle |
p120-Catenin is essential for N-cadherin-mediated formation of proper junctional structure, thereby establishing cell polarity in epithelial cells.
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pubmed:affiliation |
Department of Bioscience, School of Science and Technology, Kwansei Gakuin University, Sanda-shi, Hyogo-ken, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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