pubmed-article:12510194 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12510194 | lifeskim:mentions | umls-concept:C0221908 | lld:lifeskim |
pubmed-article:12510194 | lifeskim:mentions | umls-concept:C1180347 | lld:lifeskim |
pubmed-article:12510194 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:12510194 | lifeskim:mentions | umls-concept:C0596963 | lld:lifeskim |
pubmed-article:12510194 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:12510194 | lifeskim:mentions | umls-concept:C0872241 | lld:lifeskim |
pubmed-article:12510194 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:12510194 | pubmed:dateCreated | 2003-1-3 | lld:pubmed |
pubmed-article:12510194 | pubmed:abstractText | Polarized cells contain numerous membrane domains, but it is unclear how the formation of these domains is coordinated to create a single integrated cell architecture. Genetic screens of Drosophila melanogaster embryos have identified three complexes, each containing one of the PDZ domain proteins--Stardust (Sdt), Bazooka (Baz) and Scribble (Scrib)--that control epithelial polarity and formation of zonula adherens. We find that these complexes can be ordered into a single regulatory hierarchy that is initiated by cell adhesion-dependent recruitment of the Baz complex to the zonula adherens. The Scrib complex represses apical identity along basolateral surfaces by antagonizing Baz-initiated apical polarity. The Sdt-containing Crb complex is recruited apically by the Baz complex to counter antagonistic Scrib activity. Thus, a finely tuned balance between Scrib and Crb complex activity sets the limits of the apical and basolateral membrane domains and positions cell junctions. Our data suggest a model in which the maturation of epithelial cell polarity is driven by integration of the sequential activities of PDZ-based protein complexes. | lld:pubmed |
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pubmed-article:12510194 | pubmed:language | eng | lld:pubmed |
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pubmed-article:12510194 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:12510194 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12510194 | pubmed:month | Jan | lld:pubmed |
pubmed-article:12510194 | pubmed:issn | 1465-7392 | lld:pubmed |
pubmed-article:12510194 | pubmed:author | pubmed-author:PerrimonNorbe... | lld:pubmed |
pubmed-article:12510194 | pubmed:author | pubmed-author:BilderDavidD | lld:pubmed |
pubmed-article:12510194 | pubmed:author | pubmed-author:SchoberMarkus... | lld:pubmed |
pubmed-article:12510194 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12510194 | pubmed:volume | 5 | lld:pubmed |
pubmed-article:12510194 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12510194 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12510194 | pubmed:pagination | 53-8 | lld:pubmed |
pubmed-article:12510194 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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pubmed-article:12510194 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:12510194 | pubmed:articleTitle | Integrated activity of PDZ protein complexes regulates epithelial polarity. | lld:pubmed |
pubmed-article:12510194 | pubmed:affiliation | Department of Genetics and Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USA. bilder@socrates.berkeley.edu | lld:pubmed |
pubmed-article:12510194 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12510194 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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