ArticlePloS one2013
Characterization of FUS mutations in amyotrophic lateral sclerosis using RNA-Seq.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Exploring Protein Misfolding in Amyotrophic Lateral Sclerosis: Structural and Functional Insights.Biomedicines · 2025Review
- DDX17 is involved in DNA damage repair and modifies FUS toxicity in an RGG-domain dependent manner.Acta neuropathologica · 2021Article
- Wild-Type and Mutant FUS Expression Reduce Proliferation and Neuronal Differentiation Properties of Neural Stem Progenitor Cells.International journal of molecular sciences · 2021Article
- eVIP2: Expression-based variant impact phenotyping to predict the function of gene variants.PLoS computational biology · 2021Article
- Trends in Understanding the Pathological Roles of TDP-43 and FUS Proteins.Advances in experimental medicine and biology · 2021Article
- Methylation and Expression of MutantFrontiers in cell and developmental biology · 2021Article
- SMN complex member Gemin3 self-interacts and has a functional relationship with ALS-linked proteins TDP-43, FUS and Sod1.Scientific reports · 2019Article
- EWSR1, a multifunctional protein, regulates cellular function and aging via genetic and epigenetic pathways.Biochimica et biophysica acta. Molecular basis of disease · 2019Review
- Unanchored ubiquitin chains do not lead to marked alterations in gene expression inBiology open · 2019Article
- Amyotrophic Lateral Sclerosis associated FUS mutation shortens mitochondria and induces neurotoxicity.Scientific reports · 2018Article
- A Regulatory Circuitry Between Gria2, miR-409, and miR-495 Is Affected by ALS FUS Mutation in ESC-Derived Motor Neurons.Molecular neurobiology · 2018Article
- Review
- Mutations in the Matrin 3 gene cause familial amyotrophic lateral sclerosis.Nature neuroscience · 2014Article
- TDP-43/FUS in motor neuron disease: Complexity and challenges.Progress in neurobiologyReview
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease resulting in severe muscle weakness and eventual death by respiratory failure. Although little is known about its pathogenesis, mutations in fused in sarcoma/translated in liposarcoma (FUS) are causative for familial ALS. FUS is a multifunctional protein that is involved in many aspects of RNA processing. To elucidate the role of FUS in ALS, we overexpressed wild-type and two mutant forms of FUS in HEK-293T cells, as well as knocked-down FUS expression. This was followed by RNA-Seq to identify genes which displayed differential expression or altered splicing patterns. Pathway analysis revealed that overexpression of wild-type FUS regulates ribosomal genes, whereas knock-down of FUS additionally affects expression of spliceosome related genes. Furthermore, cells expressing mutant FUS displayed global transcription patterns more similar to cells overexpressing wild-type FUS than to the knock-down condition. This observation suggests that FUS mutants do not contribute to the pathogenesis of ALS through a loss-of-function. Finally, our results demonstrate that the R521G and R522G mutations display differences in their influence on transcription and splicing. Taken together, these results provide additional insights into the function of FUS and how mutations contribute to the development of ALS.
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Registered trials
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