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Article

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

Nature communications - 27 Jan 2015

Sun Shuying, Ling Shuo-Chien, Qiu Jinsong, Albuquerque Claudio P, Zhou Yu, Tokunaga Seiya, Li Hairi, Qiu Haiyan, Bui Anh, Yeo Gene W, Huang Eric J, Eggan Kevin, Zhou Huilin, Fu Xiang-Dong, Lagier-Tourenne Clotilde, Cleveland Don W

Abstract excerpt

The RNA-binding protein FUS/TLS, mutation in which is causative of the fatal motor neuron disease amyotrophic lateral sclerosis (ALS), is demonstrated to directly bind to the U1-snRNP and SMN complexes. ALS-causative mutations in FUS/TLS are shown to abnormally enhance their interaction with SMN and dysregulate its function, including loss of Gems and altered levels of small nuclear RNAs. The same mutants are...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 25625564
DOI: 10.1038/ncomms7171
PMCID: PMC4338613

Genes

FUS

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

ALS-causative mutations in FUS/TLS confer gain and loss of function by altered association with SMN and U1-snRNP.PMID 25625564Read ↗

Functional interaction between FUS and SMN underlies SMA-like splicing changes in wild-type hFUS miceSemantic proximity Read ↗

U1 snRNP is mislocalized in ALS patient fibroblasts bearing NLS mutations in FUS and is required for motor neuron outgrowth in zebrafish.Semantic proximity Read ↗

FUS-SMN protein interactions link the motor neuron diseases ALS and SMA.Semantic proximity Read ↗

FUS/TLS deficiency causes behavioral and pathological abnormalities distinct from amyotrophic lateral sclerosis.Semantic proximity Read ↗

Aberrant interaction of FUS with the U1 snRNA provides a molecular mechanism of FUS induced amyotrophic lateral sclerosis.Semantic proximity Read ↗

Mislocalised FUS mutants stall spliceosomal snRNPs in the cytoplasm.Semantic proximity Read ↗

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

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

Mutant FUS and ELAVL4 (HuD) Aberrant Crosstalk in Amyotrophic Lateral SclerosisSemantic proximity Read ↗

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

Spliceosome integrity is defective in the motor neuron diseases ALS and SMASemantic proximity Read ↗

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

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