publication . Article . 2018

Phase separation of FUS is suppressed by its nuclear import receptor and arginine methylation.

Mario Hofweber; Saskia Hutten; Benjamin Bourgeois; Emil Spreitzer; Annika Niedner-Boblenz; Martina Schifferer; Marc-David Ruepp; Mikael Simons; Dierk Niessing; Tobias Madl; ...
Open Access German
  • Published: 19 Apr 2018
  • Publisher: Springer
Abstract
Summary Cytoplasmic FUS aggregates are a pathological hallmark in a subset of patients with frontotemporal dementia (FTD) or amyotrophic lateral sclerosis (ALS). A key step that is disrupted in these patients is nuclear import of FUS mediated by the import receptor Transportin/Karyopherin-β2. In ALS-FUS patients, this is caused by mutations in the nuclear localization signal (NLS) of FUS that weaken Transportin binding. In FTD-FUS patients, Transportin is aggregated, and post-translational arginine methylation, which regulates the FUS-Transportin interaction, is lost. Here, we show that Transportin and arginine methylation have a crucial function beyond nuclear ...
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Subjects
Medical Subject Headings: hemic and lymphatic diseases
Fields of Science and Technology classification: 03 medical and health sciences0301 basic medicine030104 developmental biology
free text keywords: Als ; Ftd ; Karyopherin-β2 (kapβ2) ; Transportin (tnpo1) ; Arginine Methylation ; Fused In Sarcoma (fus) ; Neurodegeneration ; Nuclear Import ; Phase Separation ; Stress Granules, General Biochemistry, Genetics and Molecular Biology, Biology, Karyopherin, chemistry.chemical_classification, chemistry, Cell biology, NLS, Nuclear transport, Nuclear localization sequence, Neurodegeneration, medicine.disease, medicine, Arginine, Methylation, Stress granule
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