beta-catenin is O-GlcNAc glycosylated at Serine 23: implications for beta-catenin's subcellular localization and transactivator function.
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Ha JR, Hao L, Venkateswaran G, Huang YH, Garcia E, Persad S
beta-catenin is O-GlcNAc glycosylated at Serine 23: implications for beta-catenin's subcellular localization and transactivator function.
Exp Cell Res. 2014 Feb 15;321(2):153-66. doi: 10.1016/j.yexcr.2013.11.021. Epub 2013 Dec 14.
- PubMed ID
- 24342833 [ View in PubMed]
- Abstract
BACKGROUND: We have previously reported that beta-catenin is post-translationally modified with a single O-linked attachment of beta-N-acetyl-glucosamine (O-GlcNAc). We showed that O-GlcNAc regulated beta-catenin's subcellular localization and transcriptional activity. OBJECTIVE: The objectives of this investigation were to identify the putative O-GlcNAc sites of beta-catenin and the relevance of identified sites in the regulation of beta-catenin's localization and transcriptional activity. METHOD: Missense mutations were introduced to potential O-GlcNAc sites of pEGFP-C2-N-Terminal- or pEGFP-C2-Wild Type-beta-catenin by site-directed mutagenesis. We determined the levels of O-GlcNAc-beta-catenin, subcellular localization, interaction with binding partners and transcriptional activity of the various constructs. RESULTS: Serine 23 of beta-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. SIGNIFICANCE: O-GlcNAcylation of Serine 23 is a novel regulatory modification for beta-catenin's subcellular localization and transcriptional activity. This study is the first report to characterize site specific regulation of beta-catenin by the O-GlcNAc modification.