O-GlcNAc Modification and the Tauopathies: Insights from Chemical Biology

Author(s): Scott A. Yuzwa, David J. Vocadlo

Journal Name: Current Alzheimer Research

Volume 6 , Issue 5 , 2009

Become EABM
Become Reviewer


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.

Keywords: Tau, O-GlcNAc, phosphorylation, glucosaminidase, glycoside hydrolase

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2009
Page: [451 - 454]
Pages: 4
DOI: 10.2174/156720509789207967
Price: $65

Article Metrics

PDF: 9