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Medical AI Inquiry: You was designed to assist in medical decision-making based on the provided user questions. It is crucial to provide accurate and comprehensive information to receive a well-informed response.  Labels: BACKGROUND, OBJECTIVE, METHODS, RESULTS. Meshes: Acetylglucosamine, Glycosylation, Humans, Phosphorylation, Protein Binding, Protein Processing, Post-Translational, Protein Structure, Tertiary, Protein Transport, Serine, Tissue Distribution, Trans-Activators, Transcriptional Activation, Tumor Cells, Cultured, beta Catenin.
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Is β-catenin O-GlcNAc glycosylated at Serine 23 : implications for β-catenin 's subcellular localization and transactivator function? Context: We have previously reported that β-catenin is post-translationally modified with a single O-linked attachment of β-N-acetyl-glucosamine (O-GlcNAc). We showed that O-GlcNAc regulated β-catenin's subcellular localization and transcriptional activity. The objectives of this investigation were to identify the putative O-GlcNAc sites of β-catenin and the relevance of identified sites in the regulation of β-catenin's localization and transcriptional activity. Missense mutations were introduced to potential O-GlcNAc sites of pEGFP-C2-N-Terminal- or pEGFP-C2-Wild Type-β-catenin by site-directed mutagenesis. We determined the levels of O-GlcNAc-β-catenin, subcellular localization, interaction with binding partners and transcriptional activity of the various constructs. Serine 23 of β-catenin was determined as a site for O-GlcNAc modification which regulated its subcellular distribution, its interactions with cellular partners and consequently its transcriptional activity.
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O-GlcNAcylation of Serine 23 is a novel regulatory modification for β-catenin's subcellular localization and transcriptional activity. This study is the first report to characterize site specific regulation of β-catenin by the O-GlcNAc modification. Final Decision: yes