ArticleHuman molecular genetics2015
Subcellular localization and RNAs determine FUS architecture in different cellular compartments.
Article in Human molecular genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 27 citations in OpenAlex.
- Pathological Involvement of Protein Phase Separation and Aggregation in Neurodegenerative Diseases.International journal of molecular sciences · 2024Review
- The roles of FUS-RNA binding domain and low complexity domain in RNA-dependent phase separation.Structure (London, England : 1993) · 2024Article
- Yin and yang regulation of stress granules by Caprin-1.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Ectopic biomolecular phase transitions: fusion proteins in cancer pathologies.Trends in cell biology · 2022Review
- Homozygous ALS-linked FUS P525L mutations cell- autonomously perturb transcriptome profile and chemoreceptor signaling in human iPSC microglia.Stem cell reports · 2022Article
- Potential Therapeutic Role of HDAC Inhibitors in FUS-ALS.Frontiers in molecular neuroscience · 2021Review
- Invited Review: The role of prion-like mechanisms in neurodegenerative diseases.Neuropathology and applied neurobiology · 2020Review
- Lysine acetylation regulates the RNA binding, subcellular localization and inclusion formation of FUS.Human molecular genetics · 2020Article
- Role of circular RNAs in brain development and CNS diseases.Progress in neurobiology · 2020Review
- ALS mutations of FUS suppress protein translation and disrupt the regulation of nonsense-mediated decay.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Nuclear egress of TDP-43 and FUS occurs independently of Exportin-1/CRM1.Scientific reports · 2018Article
- Clinical and experimental studies of a novel P525R FUS mutation in amyotrophic lateral sclerosis.Neurology. Genetics · 2017Article
- Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation.Nature communications · 2017Article
- Mechanisms of Long Non-Coding RNAs in the Assembly and Plasticity of Neural Circuitry.Frontiers in neural circuits · 2017Review
- FUS interacts with nuclear matrix-associated protein SAFB1 as well as Matrin3 to regulate splicing and ligand-mediated transcription.Scientific reports · 2016Article
- Distinct and shared functions of ALS-associated proteins TDP-43, FUS and TAF15 revealed by multisystem analyses.Nature communications · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Mutations in Fused in sarcoma (FUS) gene cause a subset of familial amyotrophic lateral sclerosis (ALS), a fatal motor neuron degenerative disease. Wild-type FUS is largely localized in the nucleus, but mutant FUS accumulates in the cytoplasm and forms inclusions. It is unclear whether FUS depletion from the nucleus or FUS inclusions in the cytoplasm triggers motor neuron degeneration. In this study, we revealed that the nuclear and cytoplasmic FUS proteins form distinct local distribution patterns. The nuclear FUS forms oligomers and appears granular under confocal microscope. In contrast, the cytoplasmic FUS forms inclusions with no oligomers detected. These patterns are determined by the subcellular localization of FUS, regardless of wild-type or mutant protein. Moreover, mutant FUS remained or re-directed in the nucleus can oligomerize and behave similarly to the wild-type FUS protein. We further found that nuclear RNAs are critical to its oligomerization. Interestingly, the formation of cytoplasmic FUS inclusions is also dependent on RNA binding. Since the ALS mutations disrupt the nuclear localization sequence, mutant FUS is likely retained in the cytoplasm after translation and interacts with cytoplasmic RNAs. We therefore propose that local RNA molecules interacting with the FUS protein in different subcellular compartments play a fundamental role in determining FUS protein architecture and function.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.