title: Post-translational modifications of tau protein: implications for Alzheimer's disease.
abstract: Alzheimer's disease (AD) belongs to a group of neurodegenerative diseases collectively designated as "tauopathies", because they are characterized by the aggregation of abnormally phosphorylated tau protein. The mechanisms responsible for tau aggregation and its contribution to neurodegeneration are still unknown. Thereby, understanding the modes of regulation of tau is of high interest in the determination of the possible causes at the origin of the formation of tau aggregates and to elaborate protection strategies to cope with these pathological lesions. The regulation of tau takes place predominantly through post-translational modifications. Extensive reports have been published about tau phosphorylation; however, the other tau post-translational modifications have received much less attention. Here, we review the different types of post-translational modifications of tau including phosphorylation, glycosylation, glycation, prolyl-isomerization, cleavage or truncation, nitration, polyamination, ubiquitination, sumoylation, oxidation and aggregation, with a particular interest towards their relevance in AD.
authors.affiliation: Groupe de Neurobiologie Cellulaire-EA3842 Homéostasie cellulaire et pathologies, Faculté de Médecine, Limoges, France. lmartin.phd@gmail.com
authors.forename: Ludovic
authors.initials: L
authors.lastname: Martin
authors.forename: Xenia
authors.initials: X
authors.lastname: Latypova
authors.forename: Faraj
authors.initials: F
authors.lastname: Terro
mesh_terms: D000544:Alzheimer Disease / Q000378:metabolism*; D000818:Animals; D006801:Humans; D011499:Protein Processing, Post-Translational; D016875:tau Proteins / Q000378:metabolism*
chemical_list: D016875:tau Proteins