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Permanent link (DOI): https://doi.org/10.7939/R3ZK55V6G

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β-catenin is O-GlcNAc modified at Serine 23: Implications for β-catenin’s Subcellular Distribution and Transcriptional Activity Open Access

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Other title
Subject/Keyword
β-catenin
β-catenin is O-GlcNAc modified at Serine 23
O-GlcNAcylation
Type of item
Thesis
Degree grantor
University of Alberta
Author or creator
Ha, Jacqueline R
Supervisor and department
Persad, Sujata (Paediatrics)
Examining committee member and department
Baksh, Shairaz (Paediatrics)
Moore, Ronald (Surgery)
Pasdar, Manijeh (Cell Biology)
Department
Medical Sciences-Paediatrics
Specialization
Medical Sciences-Paediatrics
Date accepted
2012-07-27T10:34:19Z
Graduation date
2012-11
Degree
Master of Science
Degree level
Master's
Abstract
β-catenin is a potent oncoprotein that serves as a structural anchor at the adherens junctions and as a transcriptional co-activator of the Wnt Signaling pathway. β-catenin was identified to be post-translationally modified by O-linked β-D-N-acetyl-glucosamine (O-GlcNAc). This investigation was aimed to identify Serine 23 (Ser23) as a site for O-GlcNAc modification and to characterize the relevance of this site for β-catenin’s function. Serine 23 to Glycine mutant or wild-type β-catenin constructs were expressed in DU145 cell line and subsequently treated with PUGNAc—a drug that globally increases O-GlcNAcylation. O-GlcNAc-β-catenin levels were characterized by Wheat Germ Agglutinin (WGA)-HRP or WGA-agarose precipitation. Alterations in β-catenin’s subcellular localization, interactions, and transcriptional activity were analyzed through confocal microscopy, immunoprecipitation, and, RT-qPCR and luciferase reporter assay, respectively. This study demonstrated that Ser23 of β-catenin was a site for O-GlcNAcylation which increased β-catenin’s localization to the plasma membrane and decreased its transcriptional activity within the nucleus.
Language
English
DOI
doi:10.7939/R3ZK55V6G
Rights
Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of these terms. The author reserves all other publication and other rights in association with the copyright in the thesis and, except as herein before provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission.
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