Journal
CELL REPORTS
Volume 24, Issue 3, Pages 529-+Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2018.06.070
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Funding
- KU Leuven
- VIB
- European Research Council (Euro-MOTOR) [259867]
- European Research Council (ERC) [340429]
- Thierry Latran Foundation
- Fund for Scientific Research Flanders (FWO-Vlaanderen)
- Interuniversity Attraction Poles Programme [P7/16]
- Association Belge contre les Maladies Neuro-Musculaires (ABMM)
- ALS Liga (Belgium)
- Opening the Future'' Fund
- EMF/AFAR fellowship
- AARF
- Target ALS Springboard Fellowship
- Target ALS
- Packard Center for ALS Research
- ALSA
- NIH [R21NS090205]
- E. von Behring Chair for Neuromuscular and Neurodegenerative Disorders
- Hart voor ALS'' Fund, KU Leuven
- Alzheimer Research Foundation (SAO-FRA)
- Flemish Government
- European Union Joint Programme-Neurodegenerative Disease Research (JPND) Project RiMod-FTD
- European Research Council under the European Union's Horizon 2020 Framework Programme ERC [647458]
- KU Leuven (Industrieel Onderzoeksfonds'')
- Flanders Agency for Innovation by Science and Technology (IWT) (SBO Grant) [60839]
- Agency for Innovation by Science and Technology (IWT)
- EMBO long-term fellowship
- FWO-Vlaanderen
- ALSA grant [2169]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM099836] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [R21NS090205] Funding Source: NIH RePORTER
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RNA-binding protein aggregation is a pathological hallmark of several neurodegenerative disorders, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). To gain better insight into the molecular interactions underlying this process, we investigated FUS, which is mutated and aggregated in both ALS and FTLD. We generated a Drosophila model of FUS toxicity and identified a previously unrecognized synergistic effect between the N-terminal prion-like domain and the C-terminal arginine-rich domain to mediate toxicity. Although the prion-like domain is generally considered to mediate aggregation of FUS, we find that arginine residues in the C-terminal low-complexity domain are also required for maturation of FUS in cellular stress granules. These data highlight an important role for arginine-rich domains in the pathology of RNA-binding proteins.
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