Source:http://linkedlifedata.com/resource/pubmed/id/14653998
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
23
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pubmed:dateCreated |
2003-12-5
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pubmed:abstractText |
The mammalian homologs of the C. elegans partitioning-defective (Par) proteins have been demonstrated to be necessary for establishment of cell polarity. In mammalian epithelia, the Par3/Par6/aPKC polarity complex is localized to the tight junction and regulates its formation and positioning with respect to basolateral and apical membrane domains. Here we demonstrate a previously undescribed phosphorylation-dependent interaction between a mammalian homolog of the C. elegans polarity protein Par5, 14-3-3, and the tight junction-associated protein Par3. We identify phosphorylated serine 144 as a site of 14-3-3 binding. Expression of a Par3 mutant that contains serine 144 mutated to alanine (S144A) results in defects in epithelial cell polarity. In addition, overexpression of 14-3-3zeta results in a severe disruption of polarity, whereas overexpression of a 14-3-3 mutant that is defective in binding to phosphoproteins has no effect on cell polarity. Together, these data suggest a novel, phosphorylation-dependent mechanism that regulates the function of the Par3/Par6/aPKC polarity complex through 14-3-3 binding.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0960-9822
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2082-90
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14653998-14-3-3 Proteins,
pubmed-meshheading:14653998-Animals,
pubmed-meshheading:14653998-Blotting, Western,
pubmed-meshheading:14653998-Carrier Proteins,
pubmed-meshheading:14653998-Cell Polarity,
pubmed-meshheading:14653998-Cells, Cultured,
pubmed-meshheading:14653998-Epithelium,
pubmed-meshheading:14653998-Gene Expression,
pubmed-meshheading:14653998-Immunohistochemistry,
pubmed-meshheading:14653998-Mammals,
pubmed-meshheading:14653998-Phosphorylation,
pubmed-meshheading:14653998-Precipitin Tests,
pubmed-meshheading:14653998-Tight Junctions,
pubmed-meshheading:14653998-Tyrosine 3-Monooxygenase
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pubmed:year |
2003
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pubmed:articleTitle |
Phosphorylation-dependent binding of 14-3-3 to the polarity protein Par3 regulates cell polarity in mammalian epithelia.
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pubmed:affiliation |
Howard Hughes Medical Institute, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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