{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Li J"],"funding":["Science, Technology and Innovation Commission of Shenzhen Municipality","National Natural Science Foundation of China","Beijing Municipal Commission of Education","Applied Basic Research Foundation of Yunnan Province"],"pagination":["105354"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10654028"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["299(11)"],"pubmed_abstract":["O-linked N-acetylglucosamine (O-GlcNAc) glycosylation, a prevalent protein post-translational modification (PTM) that occurs intracellularly, has been shown to crosstalk with phosphorylation and ubiquitination. However, it is unclear whether it interplays with other PTMs. Here we studied its relationship with ADP-ribosylation, which involves decorating target proteins with the ADP-ribose moiety. We discovered that the poly(ADP-ribosyl)ation \"eraser\", ADP-ribose glycohydrolase (PARG), is O-GlcNAcylated at Ser26, which is in close proximity to its nuclear localization signal. O-GlcNAcylation of PARG promotes nuclear localization and chromatin association. Upon DNA damage, O-GlcNAcylation augments the recruitment of PARG to DNA damage sites and interacting with proliferating cell nuclear anti"],"journal":["The Journal of biological chemistry"],"pubmed_title":["O-GlcNAc has crosstalk with ADP-ribosylation via PARG."],"pmcid":["PMC10654028"],"funding_grant_id":["32271285","JCYJ201805073000163","202101AV070002","KZ202210028043","31872720"],"pubmed_authors":["Li J","Zheng X","Wu C","Zhou W","Liu X","Zhao S","Peng B","Wu S","Feng T","Meng L","Chen X","Xu X","Sun J"],"additional_accession":[]},"is_claimable":false,"name":"O-GlcNAc has crosstalk with ADP-ribosylation via PARG.","description":"O-linked N-acetylglucosamine (O-GlcNAc) glycosylation, a prevalent protein post-translational modification (PTM) that occurs intracellularly, has been shown to crosstalk with phosphorylation and ubiquitination. However, it is unclear whether it interplays with other PTMs. Here we studied its relationship with ADP-ribosylation, which involves decorating target proteins with the ADP-ribose moiety. We discovered that the poly(ADP-ribosyl)ation \"eraser\", ADP-ribose glycohydrolase (PARG), is O-GlcNAcylated at Ser26, which is in close proximity to its nuclear localization signal. O-GlcNAcylation of PARG promotes nuclear localization and chromatin association. Upon DNA damage, O-GlcNAcylation augments the recruitment of PARG to DNA damage sites and interacting with proliferating cell nuclear anti","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Nov","modification":"2026-05-13T14:40:00.758Z","creation":"2025-04-06T02:39:17.956Z"},"accession":"S-EPMC10654028","cross_references":{"pubmed":["37858678"],"doi":["10.1016/j.jbc.2023.105354"]}}