<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Yu F</submitter><funding>National Key R&amp;D Program of China</funding><funding>National Natural Science Foundation of China</funding><funding>National Key Research and Development Program of China</funding><pagination>e2303545</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10754140</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>10(36)</volume><pubmed_abstract>O-GlcNAcylation functions as a cellular nutrient and stress sensor and participates in almost all cellular processes. However, it remains unclear whether O-GlcNAcylation plays a role in the establishment and maintenance of cell polarity, because mice lacking O-GlcNAc transferase (OGT) are embryonically lethal. Here, a mild Ogt knockout mouse model is constructed and the important role of O-GlcNAcylation in establishing and maintaining cell polarity is demonstrated. Ogt knockout leads to severe pulmonary fibrosis and dramatically promotes epithelial-to-mesenchymal transition. Mechanistic studies reveal that OGT interacts with pericentriolar material 1 (PCM1) and centrosomal protein 131 (CEP131), components of centriolar satellites required for anchoring microtubules to the centrosome. These</pubmed_abstract><journal>Advanced science (Weinheim, Baden-Wurttemberg, Germany)</journal><pubmed_title>O-GlcNAcylation Regulates Centrosome Behavior and Cell Polarity to Reduce Pulmonary Fibrosis and Maintain the Epithelial Phenotype.</pubmed_title><pmcid>PMC10754140</pmcid><funding_grant_id>31991193</funding_grant_id><funding_grant_id>32100549</funding_grant_id><funding_grant_id>32230025</funding_grant_id><funding_grant_id>2021YFA1101001</funding_grant_id><pubmed_authors>Chen Q</pubmed_authors><pubmed_authors>Liu L</pubmed_authors><pubmed_authors>Heng D</pubmed_authors><pubmed_authors>Li D</pubmed_authors><pubmed_authors>Ni H</pubmed_authors><pubmed_authors>Yang M</pubmed_authors><pubmed_authors>Yu F</pubmed_authors><pubmed_authors>An D</pubmed_authors><pubmed_authors>Zhang X</pubmed_authors><pubmed_authors>Cao Y</pubmed_authors><pubmed_authors>Zhu X</pubmed_authors><pubmed_authors>Pei Y</pubmed_authors><pubmed_authors>Liu D</pubmed_authors><pubmed_authors>Pan L</pubmed_authors><pubmed_authors>Yang S</pubmed_authors><pubmed_authors>Wu X</pubmed_authors><pubmed_authors>Zhou J</pubmed_authors></additional><is_claimable>false</is_claimable><name>O-GlcNAcylation Regulates Centrosome Behavior and Cell Polarity to Reduce Pulmonary Fibrosis and Maintain the Epithelial Phenotype.</name><description>O-GlcNAcylation functions as a cellular nutrient and stress sensor and participates in almost all cellular processes. However, it remains unclear whether O-GlcNAcylation plays a role in the establishment and maintenance of cell polarity, because mice lacking O-GlcNAc transferase (OGT) are embryonically lethal. Here, a mild Ogt knockout mouse model is constructed and the important role of O-GlcNAcylation in establishing and maintaining cell polarity is demonstrated. Ogt knockout leads to severe pulmonary fibrosis and dramatically promotes epithelial-to-mesenchymal transition. Mechanistic studies reveal that OGT interacts with pericentriolar material 1 (PCM1) and centrosomal protein 131 (CEP131), components of centriolar satellites required for anchoring microtubules to the centrosome. These</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Dec</publication><modification>2025-04-04T12:19:37.425Z</modification><creation>2025-04-04T12:19:37.425Z</creation></dates><accession>S-EPMC10754140</accession><cross_references><pubmed>37963851</pubmed><doi>10.1002/advs.202303545</doi></cross_references></HashMap>