The Triple-Repeat Protein Anakonda Controls Epithelial Tricellular Junction Formation in Drosophila
| Autor: | Jimit Shah, Bernard Moussian, Sunitha Byri, Jade Glashauser, Tinri Aegerter-Wilmsen, Stefan Luschnig, Till Matzat, Tvisha Misra, Anne Uv, Tilmann Bätz, Zulfeqhar A. Syed, Lukas Boril |
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| Přispěvatelé: | University of Zurich, Uv, Anne |
| Rok vydání: | 2014 |
| Předmět: |
Repetitive Sequences
Amino Acid Embryo Nonmammalian Immunoblotting Septate junctions Nerve Tissue Proteins Biology Cell junction General Biochemistry Genetics and Molecular Biology Epithelium Tight Junctions 1309 Developmental Biology 1307 Cell Biology Animals Genetically Modified 03 medical and health sciences 0302 clinical medicine 1300 General Biochemistry Genetics and Molecular Biology 1312 Molecular Biology Animals Drosophila Proteins Molecular Biology 030304 developmental biology 0303 health sciences Tight junction Membrane Proteins Cell Biology Transmembrane protein 10124 Institute of Molecular Life Sciences Cell biology Transport protein Protein Transport Drosophila melanogaster Intercellular Junctions Membrane protein Cytoplasm Mutation 570 Life sciences biology 030217 neurology & neurosurgery Drosophila Protein Developmental Biology |
| Zdroj: | Developmental Cell |
| ISSN: | 1878-1551 |
| Popis: | SummaryIn epithelia, specialized tricellular junctions (TCJs) mediate cell contacts at three-cell vertices. TCJs are fundamental to epithelial biology and disease, but only a few TCJ components are known, and how they assemble at tricellular vertices is not understood. Here we describe a transmembrane protein, Anakonda (Aka), which localizes to TCJs and is essential for the formation of tricellular, but not bicellular, junctions in Drosophila. Loss of Aka causes epithelial barrier defects associated with irregular TCJ structure and geometry, suggesting that Aka organizes cell corners. Aka is necessary and sufficient for accumulation of Gliotactin at TCJs, suggesting that Aka initiates TCJ assembly by recruiting other proteins to tricellular vertices. Aka’s extracellular domain has an unusual tripartite repeat structure that may mediate self-assembly, directed by the geometry of tricellular vertices. Conversely, Aka’s cytoplasmic tail is dispensable for TCJ localization. Thus, extracellular interactions, rather than TCJ-directed intracellular transport, appear to mediate TCJ assembly. |
| Databáze: | OpenAIRE |
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