{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yu F"],"funding":["National Key R&D Program of China","National Natural Science Foundation of China","National Key Research and Development Program of China"],"pagination":["e2303545"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10754140"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(36)"],"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"],"journal":["Advanced science (Weinheim, Baden-Wurttemberg, Germany)"],"pubmed_title":["O-GlcNAcylation Regulates Centrosome Behavior and Cell Polarity to Reduce Pulmonary Fibrosis and Maintain the Epithelial Phenotype."],"pmcid":["PMC10754140"],"funding_grant_id":["31991193","32100549","32230025","2021YFA1101001"],"pubmed_authors":["Chen Q","Liu L","Heng D","Li D","Ni H","Yang M","Yu F","An D","Zhang X","Cao Y","Zhu X","Pei Y","Liu D","Pan L","Yang S","Wu X","Zhou J"],"additional_accession":[]},"is_claimable":false,"name":"O-GlcNAcylation Regulates Centrosome Behavior and Cell Polarity to Reduce Pulmonary Fibrosis and Maintain the Epithelial Phenotype.","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","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Dec","modification":"2025-04-04T12:19:37.425Z","creation":"2025-04-04T12:19:37.425Z"},"accession":"S-EPMC10754140","cross_references":{"pubmed":["37963851"],"doi":["10.1002/advs.202303545"]}}