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Journal articles on the topic 'RNA-Binding Protein FUS'

Author: Grafiati

Published: 4 June 2021

Last updated: 26 July 2025

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1

Yoneda, Ryoma, Naomi Ueda, and Riki Kurokawa. "m6A Modified Short RNA Fragments Inhibit Cytoplasmic TLS/FUS Aggregation Induced by Hyperosmotic Stress." International Journal of Molecular Sciences 22, no. 20 (2021): 11014. http://dx.doi.org/10.3390/ijms222011014.

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Translocated in LipoSarcoma/Fused in Sarcoma (TLS/FUS) is a nuclear RNA binding protein whose mutations cause amyotrophic lateral sclerosis. TLS/FUS undergoes LLPS and forms membraneless particles with other proteins and nucleic acids. Interaction with RNA alters conformation of TLS/FUS, which affects binding with proteins, but the effect of m6A RNA modification on the TLS/FUS–RNA interaction remains elusive. Here, we investigated the binding specificity of TLS/FUS to m6A RNA fragments by RNA pull down assay, and elucidated that both wild type and ALS-related TLS/FUS mutants strongly bound to

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2

Sévigny, Myriam, Isabelle Bourdeau Julien, Janani Priya Venkatasubramani, Jeremy B. Hui, Paul A. Dutchak, and Chantelle F. Sephton. "FUS contributes to mTOR-dependent inhibition of translation." Journal of Biological Chemistry 295, no. 52 (2020): 18459–73. http://dx.doi.org/10.1074/jbc.ra120.013801.

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The amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD)–linked RNA-binding protein called FUS (fused in sarcoma) has been implicated in several aspects of RNA regulation, including mRNA translation. The mechanism by which FUS affects the translation of polyribosomes has not been established. Here we show that FUS can associate with stalled polyribosomes and that this association is sensitive to mTOR (mammalian target of rapamycin) kinase activity. Specifically, we show that FUS association with polyribosomes is increased by Torin1 treatment or when cells are cultured in nutri

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3

Schwartz, Jacob C., Elaine R. Podell, Steve S. W. Han, James D. Berry, Kevin C. Eggan, and Thomas R. Cech. "FUS is sequestered in nuclear aggregates in ALS patient fibroblasts." Molecular Biology of the Cell 25, no. 17 (2014): 2571–78. http://dx.doi.org/10.1091/mbc.e14-05-1007.

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Mutations in the RNA-binding protein FUS have been shown to cause the neurodegenerative disease amyotrophic lateral sclerosis (ALS). We investigate whether mutant FUS protein in ALS patient–derived fibroblasts affects normal FUS functions in the nucleus. We investigated fibroblasts from two ALS patients possessing different FUS mutations and a normal control. Fibroblasts from these patients have their nuclear FUS protein trapped in SDS-resistant aggregates. Genome-wide analysis reveals an inappropriate accumulation of Ser-2 phosphorylation on RNA polymerase II (RNA Pol II) near the transcripti

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4

Tyzack, Giulia E., Raphaelle Luisier, Doaa M. Taha, et al. "Widespread FUS mislocalization is a molecular hallmark of amyotrophic lateral sclerosis." Brain 142, no. 9 (2019): 2572–80. http://dx.doi.org/10.1093/brain/awz217.

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Abstract Mutations causing amyotrophic lateral sclerosis (ALS) clearly implicate ubiquitously expressed and predominantly nuclear RNA binding proteins, which form pathological cytoplasmic inclusions in this context. However, the possibility that wild-type RNA binding proteins mislocalize without necessarily becoming constituents of cytoplasmic inclusions themselves remains relatively unexplored. We hypothesized that nuclear-to-cytoplasmic mislocalization of the RNA binding protein fused in sarcoma (FUS), in an unaggregated state, may occur more widely in ALS than previously recognized. To addr

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5

Li, Yun R., Oliver D. King, James Shorter, and Aaron D. Gitler. "Stress granules as crucibles of ALS pathogenesis." Journal of Cell Biology 201, no. 3 (2013): 361–72. http://dx.doi.org/10.1083/jcb.201302044.

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Amyotrophic lateral sclerosis (ALS) is a fatal human neurodegenerative disease affecting primarily motor neurons. Two RNA-binding proteins, TDP-43 and FUS, aggregate in the degenerating motor neurons of ALS patients, and mutations in the genes encoding these proteins cause some forms of ALS. TDP-43 and FUS and several related RNA-binding proteins harbor aggregation-promoting prion-like domains that allow them to rapidly self-associate. This property is critical for the formation and dynamics of cellular ribonucleoprotein granules, the crucibles of RNA metabolism and homeostasis. Recent work co

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6

Arenas, Alexandra, Jing Chen, Lisha Kuang, et al. "Lysine acetylation regulates the RNA binding, subcellular localization and inclusion formation of FUS." Human Molecular Genetics 29, no. 16 (2020): 2684–97. http://dx.doi.org/10.1093/hmg/ddaa159.

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Abstract Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease characterized by the preferential death of motor neurons. Approximately 10% of ALS cases are familial and 90% are sporadic. Fused in sarcoma (FUS) is a ubiquitously expressed RNA-binding protein implicated in familial ALS and frontotemporal dementia (FTD). The physiological function and pathological mechanism of FUS are not well understood, particularly whether post-translational modifications play a role in regulating FUS function. In this study, we discovered that FUS was acetylated at lysine-315/316 (K315/K316) and

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7

Yasuda, Kyota, Huaye Zhang, David Loiselle, Timothy Haystead, Ian G. Macara, and Stavroula Mili. "The RNA-binding protein Fus directs translation of localized mRNAs in APC-RNP granules." Journal of Cell Biology 203, no. 5 (2013): 737–46. http://dx.doi.org/10.1083/jcb.201306058.

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RNA localization pathways direct numerous mRNAs to distinct subcellular regions and affect many physiological processes. In one such pathway the tumor-suppressor protein adenomatous polyposis coli (APC) targets RNAs to cell protrusions, forming APC-containing ribonucleoprotein complexes (APC-RNPs). Here, we show that APC-RNPs associate with the RNA-binding protein Fus/TLS (fused in sarcoma/translocated in liposarcoma). Fus is not required for APC-RNP localization but is required for efficient translation of associated transcripts. Labeling of newly synthesized proteins revealed that Fus promot

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8

Korobeynikov, Vladislav A., Alexander K. Lyashchenko, Beatriz Blanco-Redondo, Paymaan Jafar-Nejad, and Neil A. Shneider. "Antisense oligonucleotide silencing of FUS expression as a therapeutic approach in amyotrophic lateral sclerosis." Nature Medicine 28, no. 1 (2022): 104–16. http://dx.doi.org/10.1038/s41591-021-01615-z.

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AbstractFused in sarcoma (FUS) is an RNA-binding protein that is genetically and pathologically associated with rare and aggressive forms of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). To explore the mechanisms by which mutant FUS causes neurodegeneration in ALS-FTD, we generated a series of FUS knock-in mouse lines that express the equivalent of ALS-associated mutant FUSP525L and FUSΔEX14 protein. In FUS mutant mice, we show progressive, age-dependent motor neuron loss as a consequence of a dose-dependent gain of toxic function, associated with the insolubility of F

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9

Sukhanova, Maria V., Anastasia S. Singatulina, David Pastré, and Olga I. Lavrik. "Fused in Sarcoma (FUS) in DNA Repair: Tango with Poly(ADP-ribose) Polymerase 1 and Compartmentalisation of Damaged DNA." International Journal of Molecular Sciences 21, no. 19 (2020): 7020. http://dx.doi.org/10.3390/ijms21197020.

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The fused in sarcoma (FUS) protein combines prion-like properties with a multifunctional DNA/RNA-binding domain and has functions spanning the regulation of RNA metabolism, including transcription, pre-mRNA splicing, mRNA transport and translation. In addition to its roles in RNA metabolism, FUS is implicated in the maintenance of DNA integrity. In this review, we examine the participation of FUS in major DNA repair pathways, focusing on DNA repair associated with poly(ADP-ribosyl)ation events and on how the interaction of FUS with poly(ADP-ribose) may orchestrate transient compartmentalisatio

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10

Humphrey, Jack, Nicol Birsa, Carmelo Milioto, et al. "FUS ALS-causative mutations impair FUS autoregulation and splicing factor networks through intron retention." Nucleic Acids Research 48, no. 12 (2020): 6889–905. http://dx.doi.org/10.1093/nar/gkaa410.

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Abstract 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 autoregulation. We and others have recently created knockin models that overcome the overexpression problem, and have generated high depth RNA-sequencing on FUS mutants in parallel

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11

Burgute, Bhagyashri D., Vivek S. Peche, Anna-Lena Steckelberg, et al. "NKAP is a novel RS-related protein that interacts with RNA and RNA binding proteins." Nucleic Acids Research 42, no. 5 (2013): 3177–93. http://dx.doi.org/10.1093/nar/gkt1311.

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Abstract NKAP is a highly conserved protein with roles in transcriptional repression, T-cell development, maturation and acquisition of functional competency and maintenance and survival of adult hematopoietic stem cells. Here we report the novel role of NKAP in splicing. With NKAP-specific antibodies we found that NKAP localizes to nuclear speckles. NKAP has an RS motif at the N-terminus followed by a highly basic domain and a DUF 926 domain at the C-terminal region. Deletion analysis showed that the basic domain is important for speckle localization. In pull-down experiments, we identified R

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12

Ikenaka, Kensuke, Shinsuke Ishigaki, Yohei Iguchi, et al. "Characteristic Features of FUS Inclusions in Spinal Motor Neurons of Sporadic Amyotrophic Lateral Sclerosis." Journal of Neuropathology & Experimental Neurology 79, no. 4 (2020): 370–77. http://dx.doi.org/10.1093/jnen/nlaa003.

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Abstract Alterations of RNA metabolism caused by mutations in RNA-binding protein genes, such as transactivating DNA-binding protein-43 (TDP-43) and fused in sarcoma (FUS), have been implicated in the pathogenesis of amyotrophic lateral sclerosis (ALS). Unlike the accumulation of TDP43, which is accepted as a pathological hall mark of sporadic ALS (sALS), FUS pathology in sALS is still under debate. Although immunoreactive inclusions of FUS have been detected in sALS patients previously, the technical limitation of signal detection, including the necessity of specific antigen retrieval, restri

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13

Hayden, Elliott, Shuzhen Chen, Abagail Chumley, Chenyi Xia, Quan Zhong, and Shulin Ju. "A Genetic Screen for Human Genes Suppressing FUS Induced Toxicity in Yeast." G3: Genes|Genomes|Genetics 10, no. 6 (2020): 1843–52. http://dx.doi.org/10.1534/g3.120.401164.

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FUS is a nucleic acid binding protein that, when mutated, cause a subset of familial amyotrophic lateral sclerosis (ALS). Expression of FUS in yeast recapitulates several pathological features of the disease-causing mutant proteins, including nuclear to cytoplasmic translocation, formation of cytoplasmic inclusions, and cytotoxicity. Genetic screens using the yeast model of FUS have identified yeast genes and their corresponding human homologs suppressing FUS induced toxicity in yeast, neurons and animal models. To expand the search for human suppressor genes of FUS induced toxicity, we carrie

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14

Martinez-Macias, Maria Isabel, Duncan AQ Moore, Ryan L. Green, et al. "FUS (fused in sarcoma) is a component of the cellular response to topoisomerase I–induced DNA breakage and transcriptional stress." Life Science Alliance 2, no. 2 (2019): e201800222. http://dx.doi.org/10.26508/lsa.201800222.

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FUS (fused in sarcoma) plays a key role in several steps of RNA metabolism, and dominant mutations in this protein are associated with neurodegenerative diseases. Here, we show that FUS is a component of the cellular response to topoisomerase I (TOP1)–induced DNA breakage; relocalising to the nucleolus in response to RNA polymerase II (Pol II) stalling at sites of TOP1-induced DNA breaks. This relocalisation is rapid and dynamic, reversing following the removal of TOP1-induced breaks and coinciding with the recovery of global transcription. Importantly, FUS relocalisation following TOP1-induce

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15

Popper, Bastian, Tom Scheidt, and Rico Schieweck. "RNA-binding protein dysfunction in neurodegeneration." Essays in Biochemistry 65, no. 7 (2021): 975–86. http://dx.doi.org/10.1042/ebc20210024.

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Abstract Protein homeostasis (proteostasis) is a prerequisite for cellular viability and plasticity. In particular, post-mitotic cells such as neurons rely on a tightly regulated safeguard system that allows for regulated protein expression. Previous investigations have identified RNA-binding proteins (RBPs) as crucial regulators of protein expression in nerve cells. However, during neurodegeneration, their ability to control the proteome is progressively disrupted. In this review, we examine the malfunction of key RBPs such as TAR DNA-binding protein 43 (TDP-43), Fused in Sarcoma (FUS), Stauf

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16

Ugras, Scott E., and James Shorter. "RNA-Binding Proteins in Amyotrophic Lateral Sclerosis and Neurodegeneration." Neurology Research International 2012 (2012): 1–5. http://dx.doi.org/10.1155/2012/432780.

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Amyotrophic Lateral Sclerosis (ALS) is an adult onset neurodegenerative disease, which is universally fatal. While the causes of this devastating disease are poorly understood, recent advances have implicated RNA-binding proteins (RBPs) that contain predicted prion domains as a major culprit. Specifically, mutations in the RBPs TDP-43 and FUS can cause ALS. Cytoplasmic mislocalization and inclusion formation are common pathological features of TDP-43 and FUS proteinopathies. Though these RBPs share striking pathological and structural similarities, considerable evidence suggests that the ALS-l

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17

Bao, Le, Lei Yuan, Pengfei Li, et al. "A FUS-LATS1/2 Axis Inhibits Hepatocellular Carcinoma Progression via Activating Hippo Pathway." Cellular Physiology and Biochemistry 50, no. 2 (2018): 437–51. http://dx.doi.org/10.1159/000494155.

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Background/Aims: The roles and related mechanisms of RNA binding protein FUS (fused in sarcoma/translocated in liposarcoma) are unclear in numerous cancers, including hepatocellular carcinoma (HCC). Methods: Quantitative reverse transcription PCR (qRT-PCR), western blot, cell viability, transwell migration and invasion, tumor spheres formation and in vivo tumor formation assays were used to examine the effects of FUS on HCC progression in HuH7 and MHCC97 cells. Additionally, transcriptome analysis based on RNA-sequencing data, qRT-PCR, western blots, luciferase reporter and RNA binding protein

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18

Strohm, Laura, Zehan Hu, Yongwon Suk, et al. "Multi-omics profiling identifies a deregulated FUS-MAP1B axis in ALS/FTD–associated UBQLN2 mutants." Life Science Alliance 5, no. 11 (2022): e202101327. http://dx.doi.org/10.26508/lsa.202101327.

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Ubiquilin-2 (UBQLN2) is a ubiquitin-binding protein that shuttles ubiquitinated proteins to proteasomal and autophagic degradation. UBQLN2 mutations are genetically linked to the neurodegenerative disorders amyotrophic lateral sclerosis and frontotemporal dementia (ALS/FTD). However, it remains elusive how UBQLN2 mutations cause ALS/FTD. Here, we systematically examined proteomic and transcriptomic changes in patient-derived lymphoblasts and CRISPR/Cas9–engineered HeLa cells carrying ALS/FTD UBQLN2 mutations. This analysis revealed a strong up-regulation of the microtubule-associated protein 1

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19

Shelkovnikova, Tatyana A. "Modelling FUSopathies: focus on protein aggregation." Biochemical Society Transactions 41, no. 6 (2013): 1613–17. http://dx.doi.org/10.1042/bst20130212.

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The discovery of a causative link between dysfunction of a number of RNA-binding proteins with prion-like domains and the development of certain (neuro)degenerative diseases has completely changed our perception of molecular mechanisms instigating pathological process in these disorders. Irreversible aggregation of these proteins is a crucial pathogenic event delineating a type of proteinopathy. FUS (fused in sarcoma) is a prototypical member of the class, and studies into the causes and consequences of FUSopathies have been instrumental in characterizing the processes leading to deregulation

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Barmada, Sami J., Shulin Ju, Arpana Arjun, et al. "Amelioration of toxicity in neuronal models of amyotrophic lateral sclerosis by hUPF1." Proceedings of the National Academy of Sciences 112, no. 25 (2015): 7821–26. http://dx.doi.org/10.1073/pnas.1509744112.

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Over 30% of patients with amyotrophic lateral sclerosis (ALS) exhibit cognitive deficits indicative of frontotemporal dementia (FTD), suggesting a common pathogenesis for both diseases. Consistent with this hypothesis, neuronal and glial inclusions rich in TDP43, an essential RNA-binding protein, are found in the majority of those with ALS and FTD, and mutations in TDP43 and a related RNA-binding protein, FUS, cause familial ALS and FTD. TDP43 and FUS affect the splicing of thousands of transcripts, in some cases triggering nonsense-mediated mRNA decay (NMD), a highly conserved RNA degradation

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Hamad, Nesreen, Hiroki Watanabe, Takayuki Uchihashi, Riki Kurokawa, Takashi Nagata, and Masato Katahira. "Direct visualization of the conformational change of FUS/TLS upon binding to promoter-associated non-coding RNA." Chemical Communications 56, no. 64 (2020): 9134–37. http://dx.doi.org/10.1039/d0cc03776a.

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Colantoni, Alessio, Davide Capauto, Vincenzo Alfano, et al. "FUS Alters circRNA Metabolism in Human Motor Neurons Carrying the ALS-Linked P525L Mutation." International Journal of Molecular Sciences 24, no. 4 (2023): 3181. http://dx.doi.org/10.3390/ijms24043181.

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Deregulation of RNA metabolism has emerged as one of the key events leading to the degeneration of motor neurons (MNs) in Amyotrophic Lateral Sclerosis (ALS) disease. Indeed, mutations on RNA-binding proteins (RBPs) or on proteins involved in aspects of RNA metabolism account for the majority of familiar forms of ALS. In particular, the impact of the ALS-linked mutations of the RBP FUS on many aspects of RNA-related processes has been vastly investigated. FUS plays a pivotal role in splicing regulation and its mutations severely alter the exon composition of transcripts coding for proteins inv

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Hennig, Sven, Geraldine Kong, Taro Mannen, et al. "Prion-like domains in RNA binding proteins are essential for building subnuclear paraspeckles." Journal of Cell Biology 210, no. 4 (2015): 529–39. http://dx.doi.org/10.1083/jcb.201504117.

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Prion-like domains (PLDs) are low complexity sequences found in RNA binding proteins associated with the neurodegenerative disorder amyotrophic lateral sclerosis. Recently, PLDs have been implicated in mediating gene regulation via liquid-phase transitions that drive ribonucleoprotein granule assembly. In this paper, we report many PLDs in proteins associated with paraspeckles, subnuclear bodies that form around long noncoding RNA. We mapped the interactome network of paraspeckle proteins, finding enrichment of PLDs. We show that one protein, RBM14, connects key paraspeckle subcomplexes via in

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Romano, Maurizio, and Emanuele Buratti. "Targeting RNA Binding Proteins Involved in Neurodegeneration." Journal of Biomolecular Screening 18, no. 9 (2013): 967–83. http://dx.doi.org/10.1177/1087057113497256.

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Dysfunctions at the level of RNA processing have recently been shown to play a fundamental role in the pathogenesis of many neurodegenerative diseases. Several proteins responsible for these dysfunctions (TDP-43, FUS/TLS, and hnRNP A/Bs) belong to the nuclear class of heterogeneous ribonucleoproteins (hnRNPs) that predominantly function as general regulators of both coding and noncoding RNA metabolism. The discovery of the importance of these factors in mediating neuronal death has represented a major paradigmatic shift in our understanding of neurodegenerative processes. As a result, these di

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Masaki, Katsuhisa, Yoshifumi Sonobe, Ghanashyam Ghadge, et al. "RNA-binding protein altered expression and mislocalization in MS." Neurology - Neuroimmunology Neuroinflammation 7, no. 3 (2020): e704. http://dx.doi.org/10.1212/nxi.0000000000000704.

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ObjectiveTo determine whether there are nuclear depletion and cellular mislocalization of RNA-binding proteins (RBPs) transactivation response DNA-binding protein of 43 kDa (TDP-43), fused in sarcoma (FUS), and polypyrimidine tract–binding protein (PTB) in MS, as is the case in amyotrophic lateral sclerosis (ALS) and oligodendrocytes infected with Theiler murine encephalomyelitis virus (TMEV), we examined MS lesions and in vitro cultured primary human brain–derived oligodendrocytes.MethodsNuclear depletion and mislocalization of TDP-43, FUS, and PTB are thought to contribute to the pathogenesi

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Pham, Jade, Matt Keon, Samuel Brennan, and Nitin Saksena. "Connecting RNA-Modifying Similarities of TDP-43, FUS, and SOD1 with MicroRNA Dysregulation Amidst A Renewed Network Perspective of Amyotrophic Lateral Sclerosis Proteinopathy." International Journal of Molecular Sciences 21, no. 10 (2020): 3464. http://dx.doi.org/10.3390/ijms21103464.

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Beyond traditional approaches in understanding amyotrophic lateral sclerosis (ALS), multiple recent studies in RNA-binding proteins (RBPs)—including transactive response DNA-binding protein (TDP-43) and fused in sarcoma (FUS)—have instigated an interest in their function and prion-like properties. Given their prominence as hallmarks of a highly heterogeneous disease, this prompts a re-examination of the specific functional interrelationships between these proteins, especially as pathological SOD1—a non-RBP commonly associated with familial ALS (fALS)—exhibits similar properties to these RBPs i

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Zhang, Xue, Fengchao Wang, Yi Hu, et al. "In vivo stress granule misprocessing evidenced in a FUS knock-in ALS mouse model." Brain 143, no. 5 (2020): 1350–67. http://dx.doi.org/10.1093/brain/awaa076.

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Abstract Many RNA-binding proteins, including TDP-43, FUS, and TIA1, are stress granule components, dysfunction of which causes amyotrophic lateral sclerosis (ALS). However, whether a mutant RNA-binding protein disrupts stress granule processing in vivo in pathogenesis is unknown. Here we establish a FUS ALS mutation, p.R521C, knock-in mouse model that carries impaired motor ability and late-onset motor neuron loss. In disease-susceptible neurons, stress induces mislocalization of mutant FUS into stress granules and upregulation of ubiquitin, two hallmarks of disease pathology. Additionally, s

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Fahrenkrog, Birthe, and Amnon Harel. "Perturbations in Traffic: Aberrant Nucleocytoplasmic Transport at the Heart of Neurodegeneration." Cells 7, no. 12 (2018): 232. http://dx.doi.org/10.3390/cells7120232.

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Neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and Huntington’s disease (HD), are characterized by intracellular aggregation of proteins. In the case of ALS and FTD, these protein aggregates are found in the cytoplasm of affected neurons and contain certain RNA-binding proteins (RBPs), namely the TAR DNA-binding protein of 43 kDa (TDP-43) and the fused in sarcoma (FUS) gene product. TDP-43 and FUS are nuclear proteins and their displacement to the cytoplasm is thought to be adverse in at least two ways: loss-of-function in the nucleus an

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Gasperini, Lisa, Annalisa Rossi, Nicola Cornella, et al. "The hnRNP RALY regulates PRMT1 expression and interacts with the ALS-linked protein FUS: implication for reciprocal cellular localization." Molecular Biology of the Cell 29, no. 26 (2018): 3067–81. http://dx.doi.org/10.1091/mbc.e18-02-0108.

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The RBP associated with lethal yellow mutation (RALY) is a member of the heterogeneous nuclear ribonucleoprotein family whose transcriptome and interactome have been recently characterized. RALY binds poly-U rich elements within several RNAs and regulates the expression as well as the stability of specific transcripts. Here we show that RALY binds PRMT1 mRNA and regulates its expression. PRMT1 catalyzes the arginine methylation of Fused in Sarcoma (FUS), an RNA-binding protein that interacts with RALY. We demonstrate that RALY down-regulation decreases protein arginine N-methyltransferase 1 le

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Birsa, Nicol, Agnieszka M. Ule, Maria Giovanna Garone, et al. "FUS-ALS mutants alter FMRP phase separation equilibrium and impair protein translation." Science Advances 7, no. 30 (2021): eabf8660. http://dx.doi.org/10.1126/sciadv.abf8660.

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FUsed in Sarcoma (FUS) is a multifunctional RNA binding protein (RBP). FUS mutations lead to its cytoplasmic mislocalization and cause the neurodegenerative disease amyotrophic lateral sclerosis (ALS). Here, we use mouse and human models with endogenous ALS-associated mutations to study the early consequences of increased cytoplasmic FUS. We show that in axons, mutant FUS condensates sequester and promote the phase separation of fragile X mental retardation protein (FMRP), another RBP associated with neurodegeneration. This leads to repression of translation in mouse and human FUS-ALS motor ne

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Ueda, Naomi, Ryoma Yoneda, and Riki Kurokawa. "Identification of Essential Components of RNA Binding Domain of TLS/FUS." Biomedical Sciences 10, no. 2 (2024): 30–43. http://dx.doi.org/10.11648/j.bs.20241002.13.

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TLS/FUS is RNA-binding protein having multiple functions of regulations of genes, homeostasis, and cellular growth. Recent studies show that TLS is involved in phase separation and occasionally forms precipitation related to neurodegenerative diseases like amyotrophic lateral sclerosis (ALS). RNA has been reported to suppress phase separation, droplet formation, and concomitant precipitation of TLS, suggesting that RNA is a possible candidate for ALS drug discovery. Our experiments demonstrated that a long noncoding RNA, promoter-associated noncoding RNA (pncRNA-D), specifically binds TLS and

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Chen, Chen, Xiufang Ding, Nimrah Akram, Song Xue, and Shi-Zhong Luo. "Fused in Sarcoma: Properties, Self-Assembly and Correlation with Neurodegenerative Diseases." Molecules 24, no. 8 (2019): 1622. http://dx.doi.org/10.3390/molecules24081622.

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Fused in sarcoma (FUS) is a DNA/RNA binding protein that is involved in RNA metabolism and DNA repair. Numerous reports have demonstrated by pathological and genetic analysis that FUS is associated with a variety of neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), frontotemporal lobar degeneration (FTLD), and polyglutamine diseases. Traditionally, the fibrillar aggregation of FUS was considered to be the cause of those diseases, especially via its prion-like domains (PrLDs), which are rich in glutamine and asparagine residues. Lately, a nonfibrillar self-assembling ph

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Bennett, Seth A., Samantha N. Cobos, Raven M. A. Fisher, et al. "Direct and Indirect Protein Interactions Link FUS Aggregation to Histone Post-Translational Modification Dysregulation and Growth Suppression in an ALS/FTD Yeast Model." Journal of Fungi 11, no. 1 (2025): 58. https://doi.org/10.3390/jof11010058.

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Amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) are incurable neurodegenerative disorders sharing pathological and genetic features, including mutations in the FUS gene. FUS is an RNA-binding protein that mislocalizes to the cytoplasm and aggregates in ALS/FTD. In a yeast model, FUS proteinopathy is connected to changes in the epigenome, including reductions in the levels of H3S10ph, H3K14ac, and H3K56ac. Exploiting the same model, we reveal novel connections between FUS aggregation and epigenetic dysregulation. We show that the histone-modifying enzymes Ipl1 and Rtt109—r

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Alshalfie, Walaa, Maryam Fotouhi, Riham Ayoubi, et al. "The identification of high-performing antibodies for RNA-binding protein FUS for use in Western Blot, immunoprecipitation, and immunofluorescence." F1000Research 12 (June 26, 2023): 376. http://dx.doi.org/10.12688/f1000research.133220.2.

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RNA-binding protein Fused-in Sarcoma (FUS) plays an essential role in various cellular processes. Mutations in the C-terminal domain region, where the nuclear localization signal (NLS) is located, causes the redistribution of FUS from the nucleus to the cytoplasm. In neurons, neurotoxic aggregates are formed as a result, contributing to neurogenerative diseases. Well-characterized anti-FUS antibodies would enable the reproducibility of FUS research, thereby benefiting the scientific community. In this study, we characterized ten FUS commercial antibodies for Western Blot, immunoprecipitation,

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Alshalfie, Walaa, Maryam Fotouhi, Riham Ayoubi, et al. "The identification of high-performing antibodies for RNA-binding protein FUS for use in Western Blot, immunoprecipitation, and immunofluorescence." F1000Research 12 (April 6, 2023): 376. http://dx.doi.org/10.12688/f1000research.133220.1.

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RNA-binding protein Fused-in Sarcoma (FUS) plays an essential role in various cellular processes. Mutations in the C-terminal domain region, where the nuclear localization signal (NLS) is located, causes the redistribution of FUS from the nucleus to the cytoplasm. In neurons, neurotoxic aggregates are formed as a result, contributing to neurogenerative diseases. Well-characterized anti-FUS antibodies would enable the reproducibility of FUS research, thereby benefiting the scientific community. In this study, we characterized ten FUS commercial antibodies for Western Blot, immunoprecipitation,

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Markert, Sebastian M., Michael Skoruppa, Bin Yu, et al. "Overexpression of an ALS-associated FUS mutation in C. elegans disrupts NMJ morphology and leads to defective neuromuscular transmission." Biology Open 9, no. 12 (2020): bio055129. http://dx.doi.org/10.1242/bio.055129.

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ABSTRACTThe amyotrophic lateral sclerosis (ALS) neurodegenerative disorder has been associated with multiple genetic lesions, including mutations in the gene for fused in sarcoma (FUS), a nuclear-localized RNA/DNA-binding protein. Neuronal expression of the pathological form of FUS proteins in Caenorhabditis elegans results in mislocalization and aggregation of FUS in the cytoplasm, and leads to impairment of motility. However, the mechanisms by which the mutant FUS disrupts neuronal health and function remain unclear. Here we investigated the impact of ALS-associated FUS on motor neuron healt

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Yasuda, Kyota, Sarah F. Clatterbuck-Soper, Meredith E. Jackrel, James Shorter, and Stavroula Mili. "FUS inclusions disrupt RNA localization by sequestering kinesin-1 and inhibiting microtubule detyrosination." Journal of Cell Biology 216, no. 4 (2017): 1015–34. http://dx.doi.org/10.1083/jcb.201608022.

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Cytoplasmic inclusions of the RNA-binding protein fused in sarcoma (FUS) represent one type of membraneless ribonucleoprotein compartment. Formation of FUS inclusions is promoted by amyotrophic lateral sclerosis (ALS)–linked mutations, but the cellular functions affected upon inclusion formation are poorly defined. In this study, we find that FUS inclusions lead to the mislocalization of specific RNAs from fibroblast cell protrusions and neuronal axons. This is mediated by recruitment of kinesin-1 mRNA and protein within FUS inclusions, leading to a loss of detyrosinated glutamate (Glu)–microt

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Hofmann, Jeffrey W., William W. Seeley, and Eric J. Huang. "RNA Binding Proteins and the Pathogenesis of Frontotemporal Lobar Degeneration." Annual Review of Pathology: Mechanisms of Disease 14, no. 1 (2019): 469–95. http://dx.doi.org/10.1146/annurev-pathmechdis-012418-012955.

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Frontotemporal dementia is a group of early onset dementia syndromes linked to underlying frontotemporal lobar degeneration (FTLD) pathology that can be classified based on the formation of abnormal protein aggregates involving tau and two RNA binding proteins, TDP-43 and FUS. Although elucidation of the mechanisms leading to FTLD pathology is in progress, recent advances in genetics and neuropathology indicate that a majority of FTLD cases with proteinopathy involving RNA binding proteins show highly congruent genotype–phenotype correlations. Specifically, recent studies have uncovered the un

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Harley, Jasmine, and Rickie Patani. "Stress-Specific Spatiotemporal Responses of RNA-Binding Proteins in Human Stem Cell-Derived Motor Neurons." International Journal of Molecular Sciences 21, no. 21 (2020): 8346. http://dx.doi.org/10.3390/ijms21218346.

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RNA-binding proteins (RBPs) have been shown to play a key role in the pathogenesis of a variety of neurodegenerative disorders. Amyotrophic lateral sclerosis (ALS) is an exemplar neurodegenerative disease characterised by rapid progression and relatively selective motor neuron loss. Nuclear-to-cytoplasmic mislocalisation and accumulation of RBPs have been identified as a pathological hallmark of the disease, yet the spatiotemporal responses of RBPs to different extrinsic stressors in human neurons remain incompletely understood. Here, we used healthy induced pluripotent stem cell (iPSC)-derive

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Xin, Yunchao, Xiaoling Shang, Xiaoran Sun, Guogang Xu, Yachao Liu, and Yanbin Liu. "SLC8A1 antisense RNA 1 suppresses papillary thyroid cancer malignant progression via the FUS RNA binding protein (FUS)/NUMB like endocytic adaptor protein (Numbl) axis." Bioengineered 13, no. 5 (2022): 12572–82. http://dx.doi.org/10.1080/21655979.2022.2073125.

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Kovar, Heinrich. "Dr. Jekyll and Mr. Hyde: The Two Faces of the FUS/EWS/TAF15 Protein Family." Sarcoma 2011 (2011): 1–13. http://dx.doi.org/10.1155/2011/837474.

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FUS, EWS, and TAF15 form the FET family of RNA-binding proteins whose genes are found rearranged with various transcription factor genes predominantly in sarcomas and in rare hematopoietic and epithelial cancers. The resulting fusion gene products have attracted considerable interest as diagnostic and promising therapeutic targets. So far, oncogenic FET fusion proteins have been regarded as strong transcription factors that aberrantly activate or repress target genes of their DNA-binding fusion partners. However, the role of the transactivating domain in the context of the normal FET proteins

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Alshalfie, Walaa, Michael Biddle, Maryam Fotouhi, et al. "The identification of high-performing antibodies for FUS (Uniprot ID: P35637) for use in western blot, immunoprecipitation, immunofluorescence and flow cytometry." F1000Research 12 (September 24, 2024): 376. http://dx.doi.org/10.12688/f1000research.133220.3.

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RNA-binding protein Fused-in Sarcoma (FUS) plays an essential role in various cellular processes. Mutations in the C-terminal domain region, where the nuclear localization signal (NLS) is located, causes the redistribution of FUS from the nucleus to the cytoplasm. In neurons, neurotoxic aggregates are formed as a result, contributing to neurogenerative diseases. Well-characterized anti-FUS antibodies would enable the reproducibility of FUS research, thereby benefiting the scientific community. In this study, we characterized ten FUS commercial antibodies for Western Blot, immunoprecipitation,

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Harrison, Alice Ford, and James Shorter. "RNA-binding proteins with prion-like domains in health and disease." Biochemical Journal 474, no. 8 (2017): 1417–38. http://dx.doi.org/10.1042/bcj20160499.

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Approximately 70 human RNA-binding proteins (RBPs) contain a prion-like domain (PrLD). PrLDs are low-complexity domains that possess a similar amino acid composition to prion domains in yeast, which enable several proteins, including Sup35 and Rnq1, to form infectious conformers, termed prions. In humans, PrLDs contribute to RBP function and enable RBPs to undergo liquid–liquid phase transitions that underlie the biogenesis of various membraneless organelles. However, this activity appears to render RBPs prone to misfolding and aggregation connected to neurodegenerative disease. Indeed, numero

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Doi, Hiroshi, Shigeru Koyano, Yume Suzuki, Nobuyuki Nukina, and Yoshiyuki Kuroiwa. "The RNA-binding protein FUS/TLS is a common aggregate-interacting protein in polyglutamine diseases." Neuroscience Research 66, no. 1 (2010): 131–33. http://dx.doi.org/10.1016/j.neures.2009.10.004.

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Sanchez-Burgos, Ignacio, Jorge R. Espinosa, Jerelle A. Joseph, and Rosana Collepardo-Guevara. "RNA length has a non-trivial effect in the stability of biomolecular condensates formed by RNA-binding proteins." PLOS Computational Biology 18, no. 2 (2022): e1009810. http://dx.doi.org/10.1371/journal.pcbi.1009810.

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Biomolecular condensates formed via liquid–liquid phase separation (LLPS) play a crucial role in the spatiotemporal organization of the cell material. Nucleic acids can act as critical modulators in the stability of these protein condensates. To unveil the role of RNA length in regulating the stability of RNA binding protein (RBP) condensates, we present a multiscale computational strategy that exploits the advantages of a sequence-dependent coarse-grained representation of proteins and a minimal coarse-grained model wherein proteins are described as patchy colloids. We find that for a constan

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Ling, Shuo-Chien. "Synaptic Paths to Neurodegeneration: The Emerging Role of TDP-43 and FUS in Synaptic Functions." Neural Plasticity 2018 (2018): 1–13. http://dx.doi.org/10.1155/2018/8413496.

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TAR DNA-binding protein-43 KDa (TDP-43) and fused in sarcoma (FUS) as the defining pathological hallmarks for amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), coupled with ALS-FTD-causing mutations in both genes, indicate that their dysfunctions damage the motor system and cognition. On the molecular level, TDP-43 and FUS participate in the biogenesis and metabolism of coding and noncoding RNAs as well as in the transport and translation of mRNAs as part of cytoplasmic mRNA-ribonucleoprotein (mRNP) granules. Intriguingly, many of the RNA targets of TDP-43 and FUS are invo

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Sugawara, Takeaki, Hideyuki Oguro, and Atsushi Iwama. "TET Family Oncogene Fus Is Essential for the Maintenance of Self-Renewing Hematopoietic Stem Cells." Blood 114, no. 22 (2009): 2529. http://dx.doi.org/10.1182/blood.v114.22.2529.2529.

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Abstract Abstract 2529 Poster Board II-506 A Proto-oncogene FUS (fusion derived from malignant liposarcoma), also known as TLS (translocated in liposarcoma), was originally identified in chromosomal translocation of human soft tissue sarcoma. FUS is also known to be fused with an ETS family transcription factor ERG in human myeloid leukemia with t(16;21) which is associated with poor prognosis. Based on its protein structure, DNA- and RNA-binding activity and involvement in many human cancers as the fusion with various transcription factors, FUS is now grouped with EWS and TAFII68 into TET (FE

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Tyzack, Giulia E., Jacob Neeves, Hamish Crerar, et al. "Aberrant cytoplasmic intron retention is a blueprint for RNA binding protein mislocalization in VCP-related amyotrophic lateral sclerosis." Brain 144, no. 7 (2021): 1985–93. http://dx.doi.org/10.1093/brain/awab078.

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Abstract We recently described aberrantly increased cytoplasmic SFPQ intron-retaining transcripts (IRTs) and concurrent SFPQ protein mislocalization as new hallmarks of amyotrophic lateral sclerosis (ALS). However, the generalizability and potential roles of cytoplasmic IRTs in health and disease remain unclear. Here, using time-resolved deep sequencing of nuclear and cytoplasmic fractions of human induced pluripotent stem cells undergoing motor neurogenesis, we reveal that ALS-causing VCP gene mutations lead to compartment-specific aberrant accumulation of IRTs. Specifically, we identify &amp

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Zhang, Huaiying. "Preprint Highlight: A role for phase separation to prevent R-loops during transcription." Molecular Biology of the Cell 33, no. 13 (2022). http://dx.doi.org/10.1091/mbc.p22-09-1003.

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The RNA-binding protein FUS (FUSed in sarcoma) regulates transcription by binding to polymerases and undergoing phase separation to enrich transcription machinery and RNA processing factors. Using an in vitro transcription assay and a DNA-dependent RNA polymerase from T7 phage (T7 Pol) that does not bind to FUS, this study uncovered a polymerase-binding independent role of FUS in increasing transcription productivity. The ability of FUS to phase separate with RNA prevented RNA-DNA hybrid (R-loop) formation during transcription in vitro and in cells. This work suggests a potential link between

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Wang, Yan, Xiong-Fei Zhang, Dong-Yan Wang, Yi Zhu, Lei Chen, and Jing-Jing Zhang. "Long noncoding RNA SOX2OT promotes pancreatic cancer cell migration and invasion through destabilizing FUS protein via ubiquitination." Cell Death Discovery 7, no. 1 (2021). http://dx.doi.org/10.1038/s41420-021-00640-8.

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AbstractPancreatic cancer is a highly aggressive and lethal digestive system malignancy. Our previous studies revealed the correlation of high levels of lncRNA SOX2OT expression with patients’ poor survival outcomes, the promoting role of SOX2OT in proliferation and cycle progression of pancreatic cancer cells, and the in vivo binding of SOX2OT to RNA binding protein FUS, which destabilized the protein expression of FUS. However, the mechanism of SOX2OT binding and inhibiting FUS protein stability remains unclear. In this study, we performed RNA pull-down, cycloheximide-chase, and ubiquitinati

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