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Articles

O-GlcNAc Modification of α-Synuclein Can Alter Monomer Dynamics to Control Aggregation Kinetics

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By Kasun Gamage, Binyou Wang, Eldon R. Hard, thong van
| ACS Publications
Introduction Click to copy section linkSection link copied! α-Syn can be subjected to a variety of posttranslational modifications (PTMs) that have the potential to affect the protein’s aggregation properties. (1−3) One PTM of particular interest is an intracellular form of glycosylation termed O-GlcNAc, which is the addition of the monosaccharide N-acetylglucosamine to serine and threonine residues.
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Post-translational Modification of α-Synuclein Modifies Monomer Dynamics and Aggregation Kinetics

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By Kasun Gamage, Binyou Wang, Eldon R. Hard, thong van
| BioRxiv
Abstract The intrinsically disordered protein alpha-Synuclein is identified as a major toxic aggregate in Parkinson's as well as several other neurodegenerative diseases. Recent work on this protein has focused on the effects of posttranslational modifications on aggregation kinetics. Among these, O-GlcNAcylation of alpha-Synuclein has been observed to inhibit the aggregation propensity of the protein.
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