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NMR Meets Tau: Insights into Its Function and Pathology
In this review, we focus on what we have learned from Nuclear Magnetic Resonance (NMR) studies on the neuronal microtubule-associated protein Tau. We consider both the mechanistic details of Tau: the tubulin relationship and its aggregation process. Phosphorylation of Tau is intimately linked to bot...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4919923/ https://www.ncbi.nlm.nih.gov/pubmed/27338491 http://dx.doi.org/10.3390/biom6020028 |
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author | Lippens, Guy Landrieu, Isabelle Smet, Caroline Huvent, Isabelle Gandhi, Neha S. Gigant, Benoît Despres, Clément Qi, Haoling Lopez, Juan |
author_facet | Lippens, Guy Landrieu, Isabelle Smet, Caroline Huvent, Isabelle Gandhi, Neha S. Gigant, Benoît Despres, Clément Qi, Haoling Lopez, Juan |
author_sort | Lippens, Guy |
collection | PubMed |
description | In this review, we focus on what we have learned from Nuclear Magnetic Resonance (NMR) studies on the neuronal microtubule-associated protein Tau. We consider both the mechanistic details of Tau: the tubulin relationship and its aggregation process. Phosphorylation of Tau is intimately linked to both aspects. NMR spectroscopy has depicted accurate phosphorylation patterns by different kinases, and its non-destructive character has allowed functional assays with the same samples. Finally, we will discuss other post-translational modifications of Tau and its interaction with other cellular factors in relationship to its (dys)function. |
format | Online Article Text |
id | pubmed-4919923 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-49199232016-06-24 NMR Meets Tau: Insights into Its Function and Pathology Lippens, Guy Landrieu, Isabelle Smet, Caroline Huvent, Isabelle Gandhi, Neha S. Gigant, Benoît Despres, Clément Qi, Haoling Lopez, Juan Biomolecules Review In this review, we focus on what we have learned from Nuclear Magnetic Resonance (NMR) studies on the neuronal microtubule-associated protein Tau. We consider both the mechanistic details of Tau: the tubulin relationship and its aggregation process. Phosphorylation of Tau is intimately linked to both aspects. NMR spectroscopy has depicted accurate phosphorylation patterns by different kinases, and its non-destructive character has allowed functional assays with the same samples. Finally, we will discuss other post-translational modifications of Tau and its interaction with other cellular factors in relationship to its (dys)function. MDPI 2016-06-07 /pmc/articles/PMC4919923/ /pubmed/27338491 http://dx.doi.org/10.3390/biom6020028 Text en © 2016 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Lippens, Guy Landrieu, Isabelle Smet, Caroline Huvent, Isabelle Gandhi, Neha S. Gigant, Benoît Despres, Clément Qi, Haoling Lopez, Juan NMR Meets Tau: Insights into Its Function and Pathology |
title | NMR Meets Tau: Insights into Its Function and Pathology |
title_full | NMR Meets Tau: Insights into Its Function and Pathology |
title_fullStr | NMR Meets Tau: Insights into Its Function and Pathology |
title_full_unstemmed | NMR Meets Tau: Insights into Its Function and Pathology |
title_short | NMR Meets Tau: Insights into Its Function and Pathology |
title_sort | nmr meets tau: insights into its function and pathology |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4919923/ https://www.ncbi.nlm.nih.gov/pubmed/27338491 http://dx.doi.org/10.3390/biom6020028 |
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