{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ear J"],"funding":["NCI","NIAID NIH HHS","NCI NIH HHS","NIH","NIGMS NIH HHS"],"pagination":["100859"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7005484"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(2)"],"pubmed_abstract":["Polarized distribution of organelles and molecules inside a cell is vital for a range of cellular processes and its loss is frequently encountered in disease. Polarization during planar cell migration is a special condition in which cellular orientation is triggered by cell-cell contact. We demonstrate that the protein Daple (CCDC88C) is a component of cell junctions in epithelial cells which serves like a cellular \"compass\" for establishing and maintaining contact-triggered planar polarity. Furthermore, these processes may be mediated through interaction with the polarity regulator PARD3. This interaction, mediated by Daple's PDZ-binding motif (PBM) and the third PDZ domain of PARD3, is fine-tuned by tyrosine phosphorylation on Daple's PBM by receptor and non-receptor tyrosine kinases, su"],"journal":["iScience"],"pubmed_title":["Tyrosine-Based Signals Regulate the Assembly of Daple⋅PARD3 Complex at Cell-Cell Junctions."],"pmcid":["PMC7005484"],"funding_grant_id":["R01 CA238042","R01 GM071872","CA238042","R01 CA160911","T32 CA067754","R01 GM117424","R01 AI118985","R01 CA100768","GM071872","GM117424","CA100768","AI118985","CA160911"],"pubmed_authors":["Rajapakse N","Kufareva I","Ghosh P","Ear J","Ghassemian M","Choi J","Saklecha A"],"additional_accession":[]},"is_claimable":false,"name":"Tyrosine-Based Signals Regulate the Assembly of Daple⋅PARD3 Complex at Cell-Cell Junctions.","description":"Polarized distribution of organelles and molecules inside a cell is vital for a range of cellular processes and its loss is frequently encountered in disease. Polarization during planar cell migration is a special condition in which cellular orientation is triggered by cell-cell contact. We demonstrate that the protein Daple (CCDC88C) is a component of cell junctions in epithelial cells which serves like a cellular \"compass\" for establishing and maintaining contact-triggered planar polarity. Furthermore, these processes may be mediated through interaction with the polarity regulator PARD3. This interaction, mediated by Daple's PDZ-binding motif (PBM) and the third PDZ domain of PARD3, is fine-tuned by tyrosine phosphorylation on Daple's PBM by receptor and non-receptor tyrosine kinases, su","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Feb","modification":"2026-05-07T06:46:53.807Z","creation":"2020-05-22T10:07:44Z"},"accession":"S-EPMC7005484","cross_references":{"pubmed":["32058970"],"doi":["10.1016/j.isci.2020.100859"]}}