<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Ear J</submitter><funding>NCI</funding><funding>NIAID NIH HHS</funding><funding>NCI NIH HHS</funding><funding>NIH</funding><funding>NIGMS NIH HHS</funding><pagination>100859</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7005484</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>23(2)</volume><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</pubmed_abstract><journal>iScience</journal><pubmed_title>Tyrosine-Based Signals Regulate the Assembly of Daple⋅PARD3 Complex at Cell-Cell Junctions.</pubmed_title><pmcid>PMC7005484</pmcid><funding_grant_id>R01 CA238042</funding_grant_id><funding_grant_id>R01 GM071872</funding_grant_id><funding_grant_id>CA238042</funding_grant_id><funding_grant_id>R01 CA160911</funding_grant_id><funding_grant_id>T32 CA067754</funding_grant_id><funding_grant_id>R01 GM117424</funding_grant_id><funding_grant_id>R01 AI118985</funding_grant_id><funding_grant_id>R01 CA100768</funding_grant_id><funding_grant_id>GM071872</funding_grant_id><funding_grant_id>GM117424</funding_grant_id><funding_grant_id>CA100768</funding_grant_id><funding_grant_id>AI118985</funding_grant_id><funding_grant_id>CA160911</funding_grant_id><pubmed_authors>Rajapakse N</pubmed_authors><pubmed_authors>Kufareva I</pubmed_authors><pubmed_authors>Ghosh P</pubmed_authors><pubmed_authors>Ear J</pubmed_authors><pubmed_authors>Ghassemian M</pubmed_authors><pubmed_authors>Choi J</pubmed_authors><pubmed_authors>Saklecha A</pubmed_authors></additional><is_claimable>false</is_claimable><name>Tyrosine-Based Signals Regulate the Assembly of Daple⋅PARD3 Complex at Cell-Cell Junctions.</name><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</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020 Feb</publication><modification>2026-05-07T06:46:53.807Z</modification><creation>2020-05-22T10:07:44Z</creation></dates><accession>S-EPMC7005484</accession><cross_references><pubmed>32058970</pubmed><doi>10.1016/j.isci.2020.100859</doi></cross_references></HashMap>