title: O-GlcNAc modification and the tauopathies: insights from chemical biology.
abstract: The aggregation of the microtubule-associated protein tau into paired-helical filaments is the defining characteristic of the tauopathies. It has become apparent that the hyperphosphorylation of tau likely plays a role in the aggregation process and thus strategies to reduce tau phosphorylation are generating wide interest. The O-GlcNAc posttranslational modification of tau has been shown to be reciprocal to its phosphorylation; increasing O-GlcNAc leads to reductions in tau phosphorylation. In this mini-review, we highlight the use of chemical compounds as a means of understanding the reciprocal nature of tau phosphorylation and tau O-GlcNAcylation and highlight some recent progress in this area.
authors.affiliation: Department of Molecular Biology and Biochemistry, Simon Fraser University, 8888 University Dr, Burnaby, BC, V5A 1S6, Canada.
authors.forename: Scott A
authors.initials: SA
authors.lastname: Yuzwa
authors.forename: David J
authors.initials: DJ
authors.lastname: Vocadlo
mesh_terms: D000117:Acetylglucosamine / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000378:metabolism; D016874:Neurofibrillary Tangles / Q000378:metabolism; D010766:Phosphorylation; D024801:Tauopathies / Q000378:metabolism*; D016875:tau Proteins / Q000378:metabolism*
chemical_list: D016875:tau Proteins; D000117:Acetylglucosamine