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Current Alzheimer Research

Editor-in-Chief

ISSN (Print): 1567-2050
ISSN (Online): 1875-5828

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

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

Volume 6, Issue 5, 2009

Page: [451 - 454] Pages: 4

DOI: 10.2174/156720509789207967

Price: $65

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.

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


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