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Nuclear Import Receptors Directly Bind to Arginine-Rich Dipeptide Repeat Proteins and Suppress Their Pathological Interactions

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TLDR
It is shown that arginine-rich DPRs (poly-GR and poly-PR) bind directly to multiple importins and, in excess, promote their insolubility and condensation, and suggest that importins can decrease toxicity of arginin- rich DPRs by suppressing their pathological interactions.
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This article is published in Cell Reports.The article was published on 2020-12-22 and is currently open access. It has received 58 citations till now. The article focuses on the topics: Nuclear transport & Importin.

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FUS and TDP-43 Phases in Health and Disease.

TL;DR: This paper examined how sequence, structure, post-translational modifications, and RNA can affect the self-assembly of these RNA-binding proteins (RBPs) and discussed how their emerging understanding of FUS and TDP-43 liquid-liquid phase separation (LLPS) and aggregation, could be leveraged to design new therapies for neurodegenerative diseases such as amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and limbic-predominant age-related TPD-43 encephalopathy (LATE).
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Types of nuclear localization signals and mechanisms of protein import into the nucleus.

TL;DR: In this article, the authors summarized the types of NLS, focused on the recently reported related proteins containing nuclear localization signals, and briefly summarized some mechanisms that do not depend on nuclear localization signal into the nucleus.
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Higher-order organization of biomolecular condensates.

TL;DR: In this article, a review of the underlying physical and chemical processes that generate internal condensate architectures is presented, and the authors discuss how specific condensat organization is critical for specific biological functions.
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Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation

TL;DR: Multi‐scale molecular dynamics simulations reveal reduced homotypic interactions of TDP‐43 low‐complexity domains through enhanced solvation of phosphomimetic residues, and speculate that T DP‐43 hyperphosphorylation may be a protective cellular response to counteract TDP•43 aggregation.
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Combating deleterious phase transitions in neurodegenerative disease.

TL;DR: Uversky et al. as discussed by the authors discuss the mechanisms by which aberrant protein phase transitions may contribute to neurodegenerative disease and outline potential therapeutic strategies to counter deleterious phases.
References
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Journal ArticleDOI

A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD

Alan E. Renton, +85 more
- 20 Oct 2011 - 
TL;DR: The chromosome 9p21 amyotrophic lateral sclerosis-frontotemporal dementia (ALS-FTD) locus contains one of the last major unidentified autosomal-dominant genes underlying these common neurodegenerative diseases, and a large hexanucleotide repeat expansion in the first intron of C9ORF72 is shown.
Journal ArticleDOI

A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation

TL;DR: It is proposed that liquid-like compartments carry the trade-off between functionality and risk of aggregation and that aberrant phase transitions within liquid- like compartments lie at the heart of ALS and, presumably, other age-related diseases.
Journal ArticleDOI

Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization

TL;DR: It is demonstrated that the disease-related RBP hnRNPA1 undergoes liquid-liquid phase separation (LLPS) into protein-rich droplets mediated by a low complexity sequence domain (LCD), and suggested that LCD-mediated LLPS contributes to the assembly of stress granules and their liquid properties.
Journal ArticleDOI

Decoding ALS: from genes to mechanism

TL;DR: Extraordinary progress in understanding the biology of ALS provides new reasons for optimism that meaningful therapies will be identified, and emerging themes include dysfunction in RNA metabolism and protein homeostasis, with specific defects in nucleocytoplasmic trafficking.
Related Papers (5)

A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD

Alan E. Renton, +85 more
- 20 Oct 2011 -