{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Govindan A"],"funding":["NIAID NIH HHS","NCI NIH HHS","National Institutes of Health","NIH HHS","NIGMS NIH HHS"],"pagination":["RP104439"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12017769"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13"],"pubmed_abstract":["O-GlcNAcylation is the reversible post-translational addition of β-<i>N</i>-acetylglucosamine to serine and threonine residues of nuclear and cytoplasmic proteins. It plays an important role in several cellular processes through the modification of thousands of protein substrates. O-GlcNAcylation in humans is mediated by a single essential enzyme, O-GlcNAc transferase (OGT). OGT, together with the sole O-GlcNAcase OGA, form an intricate feedback loop to maintain O-GlcNAc homeostasis in response to changes in cellular O-GlcNAc using a dynamic mechanism involving nuclear retention of its fourth intron. However, the molecular mechanism of this dynamic regulation remains unclear. Using an O-GlcNAc responsive GFP reporter cell line, we identify SFSWAP, a poorly characterized splicing factor, as"],"journal":["eLife"],"pubmed_title":["SFSWAP is a negative regulator of OGT intron detention and global pre-mRNA splicing."],"pmcid":["PMC12017769"],"funding_grant_id":["R01 GM127311","U01 CA242115","R01 AI153175","R01 AI123165"],"pubmed_authors":["Govindan A","Conrad NK"],"additional_accession":[]},"is_claimable":false,"name":"SFSWAP is a negative regulator of OGT intron detention and global pre-mRNA splicing.","description":"O-GlcNAcylation is the reversible post-translational addition of β-<i>N</i>-acetylglucosamine to serine and threonine residues of nuclear and cytoplasmic proteins. It plays an important role in several cellular processes through the modification of thousands of protein substrates. O-GlcNAcylation in humans is mediated by a single essential enzyme, O-GlcNAc transferase (OGT). OGT, together with the sole O-GlcNAcase OGA, form an intricate feedback loop to maintain O-GlcNAc homeostasis in response to changes in cellular O-GlcNAc using a dynamic mechanism involving nuclear retention of its fourth intron. However, the molecular mechanism of this dynamic regulation remains unclear. Using an O-GlcNAc responsive GFP reporter cell line, we identify SFSWAP, a poorly characterized splicing factor, as","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Apr","modification":"2026-07-15T11:03:39.645Z","creation":"2025-07-02T03:04:46.034Z"},"accession":"S-EPMC12017769","cross_references":{"pubmed":["40265571"],"doi":["10.7554/eLife.104439"]}}