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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6864
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pubmed:dateCreated |
2001-12-12
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pubmed:abstractText |
The polarized architecture of epithelial cells depends on the highly stereotypic distribution of cellular junctions and other membrane-associated protein complexes. In epithelial cells of the Drosophila embryo, three distinct domains subdivide the lateral plasma membrane. The most apical one comprises the subapical complex (SAC). It is followed by the zonula adherens (ZA) and, further basally, by the septate junction. A core component of the SAC is the transmembrane protein Crumbs, the cytoplasmic domain of which recruits the PDZ-protein Discs Lost into the complex. Cells lacking crumbs or the functionally related gene stardust fail to organize a continuous ZA and to maintain cell polarity. Here we show that stardust provides an essential component of the SAC. Stardust proteins colocalize with Crumbs and bind to the carboxy-terminal amino acids of its cytoplasmic tail. We introduce two different Stardust proteins here: one MAGUK protein, characterized by a PDZ domain, an SH3 domain and a guanylate kinase domain; and a second isoform comprising only the guanylate kinase domain. The Stardust proteins represent versatile candidates as structural and possibly regulatory constituents of the SAC, a crucial element in the control of epithelial cell polarity.
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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/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanylate Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleoside-Phosphate Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/crumbs protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/sdt protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
414
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
638-43
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pubmed:dateRevised |
2008-10-16
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pubmed:meshHeading |
pubmed-meshheading:11740560-Amino Acid Sequence,
pubmed-meshheading:11740560-Animals,
pubmed-meshheading:11740560-Animals, Genetically Modified,
pubmed-meshheading:11740560-Cell Polarity,
pubmed-meshheading:11740560-DNA, Complementary,
pubmed-meshheading:11740560-Drosophila,
pubmed-meshheading:11740560-Drosophila Proteins,
pubmed-meshheading:11740560-Embryo, Nonmammalian,
pubmed-meshheading:11740560-Epithelial Cells,
pubmed-meshheading:11740560-Guanylate Kinase,
pubmed-meshheading:11740560-Membrane Proteins,
pubmed-meshheading:11740560-Membrane Transport Proteins,
pubmed-meshheading:11740560-Molecular Sequence Data,
pubmed-meshheading:11740560-Nucleoside-Phosphate Kinase,
pubmed-meshheading:11740560-Protein Isoforms,
pubmed-meshheading:11740560-Protein Structure, Tertiary,
pubmed-meshheading:11740560-RNA, Messenger,
pubmed-meshheading:11740560-Recombinant Fusion Proteins,
pubmed-meshheading:11740560-Reverse Transcriptase Polymerase Chain Reaction
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pubmed:year |
2001
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pubmed:articleTitle |
Drosophila Stardust is a partner of Crumbs in the control of epithelial cell polarity.
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pubmed:affiliation |
Institut für Genetik, Heinrich-Heine-Universität Düsseldorf, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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