Article

Cytoplasmic accumulation of a splice variant of hnRNPA2/B1 contributes to FUS-associated toxicity in a mouse model of ALS

2024-10-21

Abstract excerpt

Genetic and experimental findings point to a crucial role of RNA dysfunction in the pathogenesis of Amyotrophic Lateral Sclerosis (ALS). Evidence suggests that mutations in RBPs such as FUS, a gene associated with ALS, affect the regulation of alternative splicing. We have previously shown that the overexpression of wild-type FUS in mice, a condition that induces ALS-like phenotypes, impacts the splicing of hnRNP...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 8276c656-b1c9-5438-8be4-c60d25284674
DOI: 10.1101/2024.10.17.618866

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Cytoplasmic accumulation of a splice variant of hnRNPA2/B1 contributes to FUS-associated toxicity in a mouse model of ALSDOI 10.1101/2024.10.17.618866Read

Cytoplasmic accumulation of a splice variant of hnRNPA2/B1 contributes to FUS-associated toxicity in a mouse model of ALSSemantic proximity Read

Cytoplasmic aggregation of mutant FUS causes multistep RNA splicing perturbations in the course of motor neuron pathology.Semantic proximity Read

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

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

Fused in sarcoma (FUS) protein lacking nuclear localization signal (NLS) and major RNA binding motifs triggers proteinopathy and severe motor phenotype in transgenic mice.Semantic proximity Read

RNA-binding ability of FUS regulates neurodegeneration, cytoplasmic mislocalization and incorporation into stress granules associated with FUS carrying ALS-linked mutationsSemantic proximity Read

Mislocated FUS is sufficient for gain-of-toxic-function amyotrophic lateral sclerosis phenotypes in mice.Semantic proximity Read

ALS-linked cytoplasmic FUS assemblies are compositionally different from physiological stress granules and sequester hnRNPA3, a novel modifier of FUS toxicity.Semantic proximity Read

Compositional analysis of ALS-linked stress granule-like structures reveals factors and cellular pathways dysregulated by mutant FUS under stressSemantic proximity Read

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

Nuclear localization sequence of FUS and induction of stress granules by ALS mutants.Semantic proximity Read

Wild-type FUS corrects ALS-like disease induced by cytoplasmic mutant FUS through autoregulationSemantic proximity Read