{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPATJ is a multi-PDZ domain scaffold protein that plays a central role in the maintenance of epithelial polarity and the formation of tight junctions. In mammalian epithelial cells, PATJ (formerly known as human INADL) interacts with components of the Crumbs complex, such as CRB3 and PALS1, thereby ensuring the integrity and spatial organization of tight junctions. Disruption of PATJ—by RNA interference or by its degradation through HPV E6 proteins—leads to mislocalization of key tight junction components including ZO-1, ZO-3, and occludin. Moreover, comparative studies with related molecules like MUPP1 highlight that PATJ is indispensable for proper junction assembly by activating the PALS1–Par6–aPKC signaling axis, and its expression also serves an important lineage marker role in differentiating ductal epithelial cells in engineered salivary tissues."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "5"}]}, {"type": "t", "text": "\n \nDirectional migration of cells is another process in which PATJ is crucial. PATJ participates in signaling complexes—such as the Amot–PATJ–Syx complex—and regulates the asymmetric distribution of proteins like aPKC and Par3 to the cell’s leading edge, contributing to coordinated cytoskeletal remodeling and directional movement during epithelial wound healing. Loss of PATJ causes mislocalization of these polarity proteins and results in defects in the orientation of the microtubule-organizing center, thereby impairing the directional migration process."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": "\n\nIn addition to its roles in cell polarity and migration, PATJ is involved in the regulation of cytokinesis. Evidence indicates that PATJ interacts with the transcription co-activator YAP at the cytokinesis midbody, where it contributes to the proper organization of the cytokinesis machinery. Disruption of PATJ or interference with its interaction with YAP leads to spindle misorientation, delayed daughter cell abscission, and consequent cytokinetic failures that may contribute to abnormal chromosomal segregation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Céline Lemmers, Emmanuelle Médina, Marie-Hélène Delgrossi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "hINADl/PATJ, a homolog of discs lost, interacts with crumbs and localizes to tight junctions in human epithelial cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M202196200"}], "href": "https://doi.org/10.1074/jbc.M202196200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11964389"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11964389"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Didier Michel, Jean-Pierre Arsanto, Dominique Massey-Harroche, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PATJ connects and stabilizes apical and lateral components of tight junctions in human intestinal cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.02528"}], "href": "https://doi.org/10.1242/jcs.02528"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16129888"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16129888"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Carina H Storrs, Saul J Silverstein "}, {"type": "b", "children": [{"type": "t", "text": "PATJ, a tight junction-associated PDZ protein, is a novel degradation target of high-risk human papillomavirus E6 and the alternatively spliced isoform 18 E6."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Virol (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/JVI.02545-06"}], "href": "https://doi.org/10.1128/JVI.02545-06"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17287269"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17287269"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Makoto Adachi, Yoko Hamazaki, Yuka Kobayashi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Similar and distinct properties of MUPP1 and Patj, two homologous PDZ domain-containing tight-junction proteins."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.01505-08"}], "href": "https://doi.org/10.1128/MCB.01505-08"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19255144"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19255144"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "D Wu, P J Chapela, C M L Barrows, et al. 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