Abstract
The accumulation of hyperphosphorylated tau is a common feature of several dementias. Tau is one of the brain microtubule – associated proteins. Here we discuss taus function in microtubule assembly and stabilization and with regards to taus interactions with other proteins, membranes, and DNA. We describe and analyze important posttranslational modifications: hyperphosphorylation, glycosylation, ubiquitination, glycation, polyamination, nitration, and truncation. We discuss how these post-translational modifications can alter taus biological function and what is known about tau self-assembly, and we propose a mechanism of tau polymerization. We analyze the impact of natural mutations on tau that cause fronto-temporal dementia associated with chromosome 17 (FTDP-1 7). Finally, we consider whether tau accumulation or its conformational change is related to tau-induced neurodegeneration, and we propose a mechanism of neurodegeneration.
Keywords: Tauopathies, hyperphosphorylated tau-proteins, dementias, Neurodegeneration, glycosylation, ubiquitination, polymerization
Current Alzheimer Research
Title: Mechanism of Tau-Induced Neurodegeneration in Alzheimer Disease and Related Tauopathies
Volume: 5 Issue: 4
Author(s): Alejandra del C. Alonso, Ben Li, Inge Grundke-Iqbal and Khalid Iqbal
Affiliation:
Keywords: Tauopathies, hyperphosphorylated tau-proteins, dementias, Neurodegeneration, glycosylation, ubiquitination, polymerization
Abstract: The accumulation of hyperphosphorylated tau is a common feature of several dementias. Tau is one of the brain microtubule – associated proteins. Here we discuss taus function in microtubule assembly and stabilization and with regards to taus interactions with other proteins, membranes, and DNA. We describe and analyze important posttranslational modifications: hyperphosphorylation, glycosylation, ubiquitination, glycation, polyamination, nitration, and truncation. We discuss how these post-translational modifications can alter taus biological function and what is known about tau self-assembly, and we propose a mechanism of tau polymerization. We analyze the impact of natural mutations on tau that cause fronto-temporal dementia associated with chromosome 17 (FTDP-1 7). Finally, we consider whether tau accumulation or its conformational change is related to tau-induced neurodegeneration, and we propose a mechanism of neurodegeneration.
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Cite this article as:
Alonso C. Alejandra del, Li Ben, Grundke-Iqbal Inge and Iqbal Khalid, Mechanism of Tau-Induced Neurodegeneration in Alzheimer Disease and Related Tauopathies, Current Alzheimer Research 2008; 5 (4) . https://dx.doi.org/10.2174/156720508785132307
DOI https://dx.doi.org/10.2174/156720508785132307 |
Print ISSN 1567-2050 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5828 |
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