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The Triple-Repeat Protein Anakonda Controls Epithelial Tricellular Junction Formation in Drosophila

Journal article
Authors Sunitha Byri
T. Misra
Zulfeqhar Ali Syed
T. Batz
J. Shah
L. Boril
J. Glashauser
T. Aegerter-Wilmsen
T. Matzat
B. Moussian
Anne Uv
S. Luschnig
Cell V. P. Ld Vj
Published in Developmental Cell
Volume 33
Issue 5
Pages 535-548
ISSN 1534-5807
Publication year 2015
Published at Institute of Biomedicine, Department of Medical and Clinical Genetics
Institute of Biomedicine
Pages 535-548
Language en
Links dx.doi.org/10.1016/j.devcel.2015.03...
Keywords TUBE-SIZE CONTROL, SEPTATE JUNCTIONS, BARRIER FUNCTION, TIGHT JUNCTIONS, DISCS LARGE, TRANSMEMBRANE PROTEIN, TRACHEAL SYSTEM, NA+/K+ ATPASE, CELLS, GLIOTACTIN, Cell Biology, Developmental Biology
Subject categories Cell and Molecular Biology

Abstract

In 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.

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