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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2005-3-1
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pubmed:abstractText |
The par (partitioning-defective) genes express a set of conserved proteins that function in polarization and asymmetric cell division. Par-3 has multiple protein-interaction domains, and associates with Par-6 and atypical protein kinase C (aPKC). In Drosophila, Par-3 is essential for epithelial cell polarization. However, its function in mammals is unclear. Here we show that depletion of Par-3 in mammalian epithelial cells profoundly disrupts tight junction assembly. Expression of a carboxy-terminal fragment plus the third PDZ domain of Par-3 partially rescues junction assembly, but neither Par-6 nor aPKC binding is required. Unexpectedly, Rac is constitutively activated in cells lacking Par-3, and the assembly of tight junctions is efficiently restored by a dominant-negative Rac mutant. The Rac exchange factor Tiam1 (ref. 7) binds directly to the carboxy-terminal region of Par-3, and knockdown of Tiam1 enhances tight junction formation in cells lacking Par-3. These results define a critical function for Par-3 in tight junction assembly, and reveal a novel mechanism through which Par-3 engages in the spatial regulation of Rac activity and establishment of epithelial polarity.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Pard3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/TIAM1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Tiam1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/cdc42 GTP-Binding Protein,
http://linkedlifedata.com/resource/pubmed/chemical/occludin
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1465-7392
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
262-9
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:15723052-Actins,
pubmed-meshheading:15723052-Animals,
pubmed-meshheading:15723052-Blotting, Western,
pubmed-meshheading:15723052-Cell Adhesion Molecules,
pubmed-meshheading:15723052-Cell Line,
pubmed-meshheading:15723052-Dogs,
pubmed-meshheading:15723052-Electroporation,
pubmed-meshheading:15723052-Epithelial Cells,
pubmed-meshheading:15723052-Epithelium,
pubmed-meshheading:15723052-Genes, Dominant,
pubmed-meshheading:15723052-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:15723052-Humans,
pubmed-meshheading:15723052-Immunoprecipitation,
pubmed-meshheading:15723052-Membrane Proteins,
pubmed-meshheading:15723052-Microscopy, Fluorescence,
pubmed-meshheading:15723052-Protein Kinase C,
pubmed-meshheading:15723052-Protein Structure, Tertiary,
pubmed-meshheading:15723052-Proteins,
pubmed-meshheading:15723052-RNA, Messenger,
pubmed-meshheading:15723052-Time Factors,
pubmed-meshheading:15723052-Transfection,
pubmed-meshheading:15723052-cdc42 GTP-Binding Protein
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pubmed:year |
2005
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pubmed:articleTitle |
Par-3 controls tight junction assembly through the Rac exchange factor Tiam1.
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pubmed:affiliation |
Center for Cell Signaling, Department of Microbiology, HSC, University of Virginia, Charlottesville, Virginia 22908, USA. xc2d@virginia.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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