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Article

Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations.

Human molecular genetics - 1 Jan 2012

Tradewell Miranda L, Yu Zhenbao, Tibshirani Michael, Boulanger Marie-Chloé, Durham Heather D, Richard Stéphane

Abstract excerpt

Mutations in FUS/TLS (fused in sarcoma/translated in liposarcoma) cause an inheritable form of amyotrophic lateral sclerosis (ALS6). In contrast to FUS(WT), which is concentrated in the nucleus, these mutants are abnormally distributed in the cytoplasm where they form inclusions and associate with stress granules. The data reported herein demonstrate the importance of protein arginine methylation in...

Read the complete abstract on PubMed

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Share to Amino Acid Motifs
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to RNA-Binding Protein FUS

Source

Identifiers

PMID: 21965298
DOI: 10.1093/hmg/ddr448

Genes

FUS
PRMT1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations.PMID 21965298Read ↗

Protein arginine methyltransferase 1 and 8 interact with FUS to modify its sub-cellular distribution and toxicity in vitro and in vivo.Semantic proximity Read ↗

Sequestration of PRMT1 and Nd1-L mRNA into ALS-linked FUS mutant R521C-positive aggregates contributes to neurite degeneration upon oxidative stress.Semantic proximity Read ↗

Nuclear import factor transportin and arginine methyltransferase 1 modify FUS neurotoxicity in Drosophila.Semantic proximity Read ↗

Intracellular localization and splicing regulation of FUS/TLS are variably affected by amyotrophic lateral sclerosis-linked mutations.Semantic proximity Read ↗

The hnRNP RALY regulates PRMT1 expression and interacts with the ALS-linked protein FUS: implication for reciprocal cellular localizationSemantic proximity Read ↗

ALS mutant FUS disrupts nuclear localization and sequesters wild-type FUS within cytoplasmic stress granules.Semantic proximity Read ↗

FUS inclusions disrupt RNA localization by sequestering kinesin-1 and inhibiting microtubule detyrosination.Semantic proximity Read ↗

Nuclear transport impairment of amyotrophic lateral sclerosis‐linked mutations in FUS/TLSSemantic proximity Read ↗

Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granulesSemantic proximity Read ↗

Toxic gain of function from mutant FUS protein is crucial to trigger cell autonomous motor neuron loss.Semantic proximity Read ↗

Cytoplasmic granule formation by FUS-R495X is attributable to arginine methylation in all Gly-rich, RGG1 and RGG2 domains.Semantic proximity Read ↗

Treatment with a Global Methyltransferase Inhibitor Induces the Intranuclear Aggregation of ALS-Linked FUS Mutant In Vitro.Semantic proximity Read ↗

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