title: Localization and Function of Pals1-associated Tight Junction Protein in Drosophila Is Regulated by Two Distinct Apical Complexes.
abstract: The transmembrane protein Crumbs (Crb) and its intracellular adaptor protein Pals1 (Stardust, Sdt in Drosophila) play a crucial role in the establishment and maintenance of apical-basal polarity in epithelial cells in various organisms. In contrast, the multiple PDZ domain-containing protein Pals1-associated tight junction protein (PATJ), which has been described to form a complex with Crb/Sdt, is not essential for apical basal polarity or for the stability of the Crb/Sdt complex in the Drosophila epidermis. Here we show that, in the embryonic epidermis, Sdt is essential for the correct subcellular localization of PATJ in differentiated epithelial cells but not during cellularization. Consistently, the L27 domain of PATJ is crucial for the correct localization and function of the protein. Our data further indicate that the four PDZ domains of PATJ function, to a large extent, in redundancy, regulating the function of the protein. Interestingly, the PATJ-Sdt heterodimer is not only recruited to the apical cell-cell contacts by binding to Crb but depends on functional Bazooka (Baz). However, biochemical experiments show that PATJ associates with both complexes, the Baz-Sdt and the Crb-Sdt complex, in the mature epithelium of the embryonic epidermis, suggesting a role of these two complexes for the function of PATJ during the development of Drosophila.
authors.affiliation: From the Institute of Molecular and Cellular Anatomy, University of Regensburg, 93053 Regensburg, Germany.
authors.forename: Arnab
authors.initials: A
authors.lastname: Sen
authors.affiliation: From the Institute of Molecular and Cellular Anatomy, University of Regensburg, 93053 Regensburg, Germany.
authors.forename: Rui
authors.initials: R
authors.lastname: Sun
authors.affiliation: From the Institute of Molecular and Cellular Anatomy, University of Regensburg, 93053 Regensburg, Germany Michael.Krahn@vkl.uni-Regensburg.de.
authors.forename: Michael P
authors.initials: MP
authors.lastname: Krahn
mesh_terms: D000818:Animals; D015153:Blotting, Western; D016764:Cell Polarity / Q000502:physiology*; D004330:Drosophila / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D029721:Drosophila Proteins / Q000235:genetics / Q000378:metabolism*; D051528:Guanylate Kinases / Q000235:genetics / Q000378:metabolism*; D007124:Immunoenzyme Techniques; D047908:Intracellular Signaling Peptides and Proteins / Q000235:genetics / Q000378:metabolism*; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000235:genetics / Q000378:metabolism*; D054731:PDZ Domains; D012333:RNA, Messenger / Q000235:genetics; D060888:Real-Time Polymerase Chain Reaction; D020133:Reverse Transcriptase Polymerase Chain Reaction; D062725:Tight Junction Proteins / Q000235:genetics / Q000378:metabolism*; D019108:Tight Junctions / Q000502:physiology
chemical_list: D029721:Drosophila Proteins; D047908:Intracellular Signaling Peptides and Proteins; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; C107903:PATJ protein, human; D012333:RNA, Messenger; D062725:Tight Junction Proteins; C400774:baz protein, Drosophila; C064360:crb protein, Drosophila; D051528:Guanylate Kinases; C444479:sdt protein, Drosophila
keywords: Drosophila; adherens junction; cell polarity; myosin; tight junction
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