PMID: 24342833

 

    Legend: Sugar

Title : β -catenin is O-GlcNAc glycosylated at Serine 23 : implications for β -catenin 's subcellular localization and transactivator function

Abstract :

1. BACKGROUND: We have previously reported that β -catenin is post-translationally modified with a single O-linked attachment of β-N-acetyl-glucosamine (O-GlcNAc).
2. We showed that O-GlcNAc regulated β -catenin 's subcellular localization and transcriptional activity
3. OBJECTIVE: 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
4. METHOD: 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
5. We determined the levels of O-GlcNAc-β-catenin, subcellular localization, interaction with binding partners and transcriptional activity of the various constructs
6. RESULTS: 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
7. SIGNIFICANCE: O-GlcNAcylation of Serine 23 is a novel regulatory modification for β -catenin 's subcellular localization and transcriptional activity
8. This study is the first report to characterize site specific regulation of β -catenin by the O-GlcNAc modification.