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

Department of Pharmacology and Molecular Therapeutics, Uniformed Services University of the Health Sciences, Bethesda, MD 20814, USA
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Int. J. Mol. Sci. 2018, 19(3), 886; https://doi.org/10.3390/ijms19030886
Received: 30 January 2018 / Revised: 5 March 2018 / Accepted: 7 March 2018 / Published: 16 March 2018
(This article belongs to the Collection Protein Folding)
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Abstract

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. View Full-Text
Keywords: FUS; ALS; FTLD; prion; amyloid; LLPS FUS; ALS; FTLD; prion; amyloid; LLPS
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
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Rhoads, S.N.; Monahan, Z.T.; Yee, D.S.; Shewmaker, F.P. The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS. Int. J. Mol. Sci. 2018, 19, 886.

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