FUS ALS-causative mutations impair FUS autoregulation and splicing factor networks through intron retention.

doi:10.1093/nar/gkaa410

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Community

Back to search

Article

FUS ALS-causative mutations impair FUS autoregulation and splicing factor networks through intron retention.

Nucleic acids research - 9 Jul 2020

Humphrey Jack, Birsa Nicol, Milioto Carmelo, McLaughlin Martha, Ule Agnieszka M, Robaldo David, Eberle Andrea B, Kräuchi Rahel, Bentham Matthew, Brown Anna-Leigh, Jarvis Seth, Bodo Cristian, Garone Maria G, Devoy Anny, Soraru Gianni, Rosa Alessandro, Bozzoni Irene, Fisher Elizabeth M C, Mühlemann Oliver, Schiavo Giampietro, Ruepp Marc-David, Isaacs Adrian M, Plagnol Vincent, Fratta Pietro

Abstract excerpt

Mutations in the RNA-binding protein FUS cause amyotrophic lateral sclerosis (ALS), a devastating neurodegenerative disease. FUS plays a role in numerous aspects of RNA metabolism, including mRNA splicing. However, the impact of ALS-causative mutations on splicing has not been fully characterized, as most disease models have been based on overexpressing mutant FUS, which will alter RNA processing due to FUS...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amyotrophic Lateral Sclerosis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytoplasm

Share to Homeostasis

Share to Loss of Function Mutation

Share to RNA-Binding Protein FUS

Share to RNA Splicing

Share to Superoxide Dismutase-1

Share to Valosin Containing Protein

Source

Open in PubMed Open full text

Identifiers

PMID: 32479602
DOI: 10.1093/nar/gkaa410
PMCID: PMC7337901

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

FUS ALS-causative mutations impair FUS autoregulation and splicing factor networks through intron retention.PMID 32479602Read ↗

<i>FUS</i> ALS-causative mutations impact <i>FUS</i> autoregulation and the processing of RNA-binding proteins through intron retentionSemantic proximity Read ↗

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

Wild-type FUS corrects ALS-like disease induced by cytoplasmic mutant FUS through autoregulation.Semantic proximity Read ↗

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

ALS-associated FUS mutations result in compromised FUS alternative splicing and autoregulation.Semantic proximity Read ↗

Characterization of FUS mutations in amyotrophic lateral sclerosis using RNA-Seq.Semantic proximity Read ↗

FUS regulates genes coding for RNA-binding proteins in neurons by binding to their highly conserved intronsSemantic proximity Read ↗

Overriding FUS autoregulation in mice triggers gain-of-toxic dysfunctions in RNA metabolism and autophagy-lysosome axisSemantic proximity Read ↗

FUS Alters circRNA Metabolism in Human Motor Neurons Carrying the ALS-Linked P525L Mutation.Semantic proximity Read ↗

Identification of a FUS splicing mutation in a large family with amyotrophic lateral sclerosis.Semantic proximity Read ↗

ALS-causative mutations in FUS/TLS confer gain and loss of function by altered association with SMN and U1-snRNP.Semantic proximity Read ↗

Amyotrophic Lateral Sclerosis associated FUS mutation shortens mitochondria and induces neurotoxicitySemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.