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First published online 23 March 2004
doi: 10.1242/jcs.01029
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Research Article |
1 Institut für Genetik, Heinrich-Heine-Universität Düsseldorf, Universitätsstr. 1, 40225 Düsseldorf, Germany
2 Leibniz Institute for Neurobiology, Department of Neurochemistry, Brenneckestr. 6, 39118 Magdeburg, Germany
3 Instituto de Ciencias Biomédicas, Facultad de Medicina, Universidad de Chile and CENI, Millenium Nucleus for Integrative Neuroscience, Santiago, Chile 6530499
4 Department of Medical Pharmacology, Center of Excellence on Neurodegenerative Diseases, University of Milan, IN-CNR, Cellular and Molecular Pharmacology Section, Italy
* Author for correspondence (e-mail: thomas{at}ifn-magdeburg.de)
Accepted 1 December 2003
Stardust (Sdt) and Discs-Large (Dlg) are membrane-associated guanylate kinases (MAGUKs) involved in the organization of supramolecular protein complexes at distinct epithelial membrane compartments in Drosophila. Loss of either Sdt or Dlg affects epithelial development with severe effects on apico-basal polarity. Moreover, Dlg is required for the structural and functional integrity of synaptic junctions. Recent biochemical and cell culture studies have revealed that various mammalian MAGUKs can interact with mLin-7/Veli/MALS, a small PDZ-domain protein. To substantiate these findings for their in vivo significance with regard to Sdt- and Dlg-based protein complexes, we analyzed the subcellular distribution of Drosophila Lin-7 (DLin-7) and performed genetic and biochemical assays to characterize its interaction with either of the two MAGUKs. In epithelia, Sdt mediates the recruitment of DLin-7 to the subapical region, while at larval neuromuscular junctions, a particular isoform of Dlg, Dlg-S97, is required for postsynaptic localization of DLin-7. Ectopic expression of Dlg-S97 in epithelia, however, was not sufficient to induce a redistribution of DLin-7. These results imply that the recruitment of DLin-7 to MAGUK-based protein complexes is defined by cell-type specific mechanisms and that DLin-7 acts downstream of Sdt in epithelia and downstream of Dlg at synapses.
Key words: Epithelial polarity, Synapse, L27 domain, Neuromuscular junction, SAP97
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