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

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

Volume: 6 Issue: 5

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

Affiliation:

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

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.

Cite this article as:

Yuzwa A. Scott and Vocadlo J. David, O-GlcNAc Modification and the Tauopathies: Insights from Chemical Biology, Current Alzheimer Research 2009; 6 (5) . https://dx.doi.org/10.2174/156720509789207967