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pubmed-article:12510194pubmed:abstractTextPolarized 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:12510194pubmed:articleTitleIntegrated activity of PDZ protein complexes regulates epithelial polarity.lld:pubmed
pubmed-article:12510194pubmed:affiliationDepartment of Genetics and Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USA. bilder@socrates.berkeley.edulld:pubmed
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