| Título: | Cell type-specific recruitment of Drosophila Lin-7 to distinct MAGUK-based protein complexes defines novel roles for Sdt and Dlg-S97 |
| Autores: |
Bachmann, André Timmer, Marco Sierralta, Jimena Pietrini, Grazia Gundelfinger, Eckart D. Knust, Elisabeth Thomas, Ulrich |
| Fecha: |
2007-04-18 2007-04-18 2004-04-15 |
| Publicador: | COMPANY OF BIOLOGISTS LTD |
| Fuente: |
Ver documento |
| Tipo: | Artículo de Revista |
| Tema: |
TUMOR-SUPPRESSOR PROTEIN EPITHELIAL-CELLS DISCS-LARGE BASOLATERAL SURFACE MAMMALIAN HOMOLOGS ADHESION SYSTEM NMDA RECEPTOR PDZ PROTEINS FASCICLIN-II POLARITY |
| Descripción: | Stardust (Sdt) and Discs-Large (Dig) 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 Dig affects epithelial development with severe effects on apico-basal polarity. Moreover, Dig 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 Dig, 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 DLin7 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 Dig at synapses. |
| Idioma: | Inglés |