Cargando…
Structural Insights Into TDP-43 and Effects of Post-translational Modifications
Transactive response DNA binding protein (TDP-43) is a key player in neurodegenerative diseases. In this review, we have gathered and presented structural information on the different regions of TDP-43 with high resolution structures available. A thorough understanding of TDP-43 structure, effect of...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6934062/ https://www.ncbi.nlm.nih.gov/pubmed/31920533 http://dx.doi.org/10.3389/fnmol.2019.00301 |
_version_ | 1783483332558848000 |
---|---|
author | François-Moutal, Liberty Perez-Miller, Samantha Scott, David D. Miranda, Victor G. Mollasalehi, Niloufar Khanna, May |
author_facet | François-Moutal, Liberty Perez-Miller, Samantha Scott, David D. Miranda, Victor G. Mollasalehi, Niloufar Khanna, May |
author_sort | François-Moutal, Liberty |
collection | PubMed |
description | Transactive response DNA binding protein (TDP-43) is a key player in neurodegenerative diseases. In this review, we have gathered and presented structural information on the different regions of TDP-43 with high resolution structures available. A thorough understanding of TDP-43 structure, effect of modifications, aggregation and sites of localization is necessary as we develop therapeutic strategies targeting TDP-43 for neurodegenerative diseases. We discuss how different domains as well as post-translational modification may influence TDP-43 overall structure, aggregation and droplet formation. The primary aim of the review is to utilize structural insights as we develop an understanding of the deleterious behavior of TDP-43 and highlight locations of established and proposed post-translation modifications. TDP-43 structure and effect on localization is paralleled by many RNA-binding proteins and this review serves as an example of how structure may be modulated by numerous compounding elements. |
format | Online Article Text |
id | pubmed-6934062 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-69340622020-01-09 Structural Insights Into TDP-43 and Effects of Post-translational Modifications François-Moutal, Liberty Perez-Miller, Samantha Scott, David D. Miranda, Victor G. Mollasalehi, Niloufar Khanna, May Front Mol Neurosci Neuroscience Transactive response DNA binding protein (TDP-43) is a key player in neurodegenerative diseases. In this review, we have gathered and presented structural information on the different regions of TDP-43 with high resolution structures available. A thorough understanding of TDP-43 structure, effect of modifications, aggregation and sites of localization is necessary as we develop therapeutic strategies targeting TDP-43 for neurodegenerative diseases. We discuss how different domains as well as post-translational modification may influence TDP-43 overall structure, aggregation and droplet formation. The primary aim of the review is to utilize structural insights as we develop an understanding of the deleterious behavior of TDP-43 and highlight locations of established and proposed post-translation modifications. TDP-43 structure and effect on localization is paralleled by many RNA-binding proteins and this review serves as an example of how structure may be modulated by numerous compounding elements. Frontiers Media S.A. 2019-12-17 /pmc/articles/PMC6934062/ /pubmed/31920533 http://dx.doi.org/10.3389/fnmol.2019.00301 Text en Copyright © 2019 François-Moutal, Perez-Miller, Scott, Miranda, Mollasalehi and Khanna. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Neuroscience François-Moutal, Liberty Perez-Miller, Samantha Scott, David D. Miranda, Victor G. Mollasalehi, Niloufar Khanna, May Structural Insights Into TDP-43 and Effects of Post-translational Modifications |
title | Structural Insights Into TDP-43 and Effects of Post-translational Modifications |
title_full | Structural Insights Into TDP-43 and Effects of Post-translational Modifications |
title_fullStr | Structural Insights Into TDP-43 and Effects of Post-translational Modifications |
title_full_unstemmed | Structural Insights Into TDP-43 and Effects of Post-translational Modifications |
title_short | Structural Insights Into TDP-43 and Effects of Post-translational Modifications |
title_sort | structural insights into tdp-43 and effects of post-translational modifications |
topic | Neuroscience |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6934062/ https://www.ncbi.nlm.nih.gov/pubmed/31920533 http://dx.doi.org/10.3389/fnmol.2019.00301 |
work_keys_str_mv | AT francoismoutalliberty structuralinsightsintotdp43andeffectsofposttranslationalmodifications AT perezmillersamantha structuralinsightsintotdp43andeffectsofposttranslationalmodifications AT scottdavidd structuralinsightsintotdp43andeffectsofposttranslationalmodifications AT mirandavictorg structuralinsightsintotdp43andeffectsofposttranslationalmodifications AT mollasalehiniloufar structuralinsightsintotdp43andeffectsofposttranslationalmodifications AT khannamay structuralinsightsintotdp43andeffectsofposttranslationalmodifications |