The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS

Subcellular mislocalization and aggregation of the human FUS protein occurs in neurons of patients with subtypes of amyotrophic lateral sclerosis and frontotemporal dementia. FUS is one of several RNA-binding proteins that can functionally self-associate into distinct liquid-phase droplet structures...

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Autores principales: Rhoads, Shannon N., Monahan, Zachary T., Yee, Debra S., Shewmaker, Frank P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5877747/
https://www.ncbi.nlm.nih.gov/pubmed/29547565
http://dx.doi.org/10.3390/ijms19030886
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author Rhoads, Shannon N.
Monahan, Zachary T.
Yee, Debra S.
Shewmaker, Frank P.
author_facet Rhoads, Shannon N.
Monahan, Zachary T.
Yee, Debra S.
Shewmaker, Frank P.
author_sort Rhoads, Shannon N.
collection PubMed
description Subcellular mislocalization and aggregation of the human FUS protein occurs in neurons of patients with subtypes of amyotrophic lateral sclerosis and frontotemporal dementia. FUS is one of several RNA-binding proteins that can functionally self-associate into distinct liquid-phase droplet structures. It is postulated that aberrant interactions within the dense phase-separated state can potentiate FUS’s transition into solid prion-like aggregates that cause disease. FUS is post-translationally modified at numerous positions, which affect both its localization and aggregation propensity. These modifications may influence FUS-linked pathology and serve as therapeutic targets.
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spelling pubmed-58777472018-04-09 The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS Rhoads, Shannon N. Monahan, Zachary T. Yee, Debra S. Shewmaker, Frank P. Int J Mol Sci Review Subcellular mislocalization and aggregation of the human FUS protein occurs in neurons of patients with subtypes of amyotrophic lateral sclerosis and frontotemporal dementia. FUS is one of several RNA-binding proteins that can functionally self-associate into distinct liquid-phase droplet structures. It is postulated that aberrant interactions within the dense phase-separated state can potentiate FUS’s transition into solid prion-like aggregates that cause disease. FUS is post-translationally modified at numerous positions, which affect both its localization and aggregation propensity. These modifications may influence FUS-linked pathology and serve as therapeutic targets. MDPI 2018-03-16 /pmc/articles/PMC5877747/ /pubmed/29547565 http://dx.doi.org/10.3390/ijms19030886 Text en © 2018 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
Rhoads, Shannon N.
Monahan, Zachary T.
Yee, Debra S.
Shewmaker, Frank P.
The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS
title The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS
title_full The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS
title_fullStr The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS
title_full_unstemmed The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS
title_short The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS
title_sort role of post-translational modifications on prion-like aggregation and liquid-phase separation of fus
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5877747/
https://www.ncbi.nlm.nih.gov/pubmed/29547565
http://dx.doi.org/10.3390/ijms19030886
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