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  • O-GlcNAc Modification Protects against Protein Misfolding and Aggregation in Neurodegenerative Disease

    Author(s)
    Ryan, Philip
    Xu, Mingming
    Davey, Andrew K
    Danon, Jonathan J
    Mellick, George D
    Kassiou, Michael
    Rudrawar, Santosh
    Griffith University Author(s)
    Rudrawar, Santosh
    Davey, Andrew
    Mellick, George
    Year published
    2019
    Metadata
    Show full item record
    Abstract
    Post-translational modifications (PTMs) of proteins are becoming the focus of intense research due to their implications in a broad spectrum of neurodegenerative diseases. Various PTMs have been identified to alter the toxic profiles of proteins which play critical roles in disease etiology. In Alzheimer’s disease (AD), dysregulated phosphorylation is reported to promote pathogenic processing of the microtubule-associated tau protein. Among the PTMs, the enzymatic addition of N-acetyl-d-glucosamine (GlcNAc) residues to Ser/Thr residues is reported to deliver protective effects against the pathogenic processing of both amyloid ...
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    Post-translational modifications (PTMs) of proteins are becoming the focus of intense research due to their implications in a broad spectrum of neurodegenerative diseases. Various PTMs have been identified to alter the toxic profiles of proteins which play critical roles in disease etiology. In Alzheimer’s disease (AD), dysregulated phosphorylation is reported to promote pathogenic processing of the microtubule-associated tau protein. Among the PTMs, the enzymatic addition of N-acetyl-d-glucosamine (GlcNAc) residues to Ser/Thr residues is reported to deliver protective effects against the pathogenic processing of both amyloid precursor protein (APP) and tau. Modification of tau with as few as one single O-GlcNAc residue inhibits its toxic self-assembly. This modification also has the same effect on the assembly of the Parkinson’s disease (PD) associated α-synuclein (ASyn) protein. In fact, O-GlcNAcylation (O-linked GlcNAc modification) affects the processing of numerous proteins implicated in AD, PD, amyotrophic lateral sclerosis (ALS), and Huntington’s disease (HD) in a similar manner. As such, manipulation of a protein’s O-GlcNAcylation status has been proposed to offer therapeutic routes toward addressing multiple neurodegenerative pathologies. Here we review the various effects that O-GlcNAc modification, and its modulated expression, have on pathogenically significant proteins involved in neurodegenerative disease.
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    Journal Title
    ACS Chemical Neuroscience
    Volume
    10
    Issue
    5
    DOI
    https://doi.org/10.1021/acschemneuro.9b00143
    Subject
    Medicinal and biomolecular chemistry
    Science & Technology
    Life Sciences & Biomedicine
    Biochemistry & Molecular Biology
    Chemistry, Medicinal
    Neurosciences
    Publication URI
    http://hdl.handle.net/10072/387158
    Collection
    • Journal articles

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