FUS/TLS forms cytoplasmic aggregates, inhibits cell growth and interacts with TDP-43 in a yeast model of amyotrophic lateral sclerosis

No abstract is available for this paper.

• Publication year

  2011

• Venue

  Protein & Cell

• Publication date

  2011-03-30

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1007/s13238-011-1525-0PMID 21452073PMCID PMC4875312
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Implications of the prion-related Q/N domains in TDP-43 and FUS

  2011cited by this paper
• Expression of human FUS/TLS in yeast leads to protein aggregation and cytotoxicity, recapitulating key features of FUS proteinopathy

  2011influential reference
• Nuclear transport impairment of amyotrophic lateral sclerosis‐linked mutations in FUS/TLS

  2011cited by this paper
• Nuclear localization sequence of FUS and induction of stress granules by ALS mutants.

  2011cited by this paper
• Suicidal [PSI+] is a lethal yeast prion

  2011cited by this paper
• TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration.

  2010cited by this paper
• FUS‐Immunoreactive Intranuclear Inclusions in Neurodegenerative Disease

  2010influential reference
• Ataxin-2 intermediate-length polyglutamine expansions are associated with increased risk for ALS

  2010cited by this paper
• Yeast as a model for studying Alzheimer's disease.

  2010cited by this paper
• Nervous yeast: modeling neurotoxic cell death.

  2010cited by this paper
• Prion-like disorders: blurring the divide between transmissibility and infectivity

  2010cited by this paper
• Amyotrophic Lateral Sclerosis-associated Proteins TDP-43 and FUS/TLS Function in a Common Biochemical Complex to Co-regulate HDAC6 mRNA*

  2010cited by this paper
• Prion amyloid structure explains templating: how proteins can be genes.

  2010cited by this paper
• Interaction with Polyglutamine Aggregates Reveals a Q/N-rich Domain in TDP-43*

  2010cited by this paper
• FUS‐immunoreactive inclusions are a common feature in sporadic and non‐SOD1 familial amyotrophic lateral sclerosis

  2010influential reference
• Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules.

  2010cited by this paper
• Modelling neurodegeneration in Saccharomyces cerevisiae: why cook with baker's yeast?

  2010cited by this paper
• ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS

  2010cited by this paper
• Mutations in FUS, an RNA Processing Protein, Cause Familial Amyotrophic Lateral Sclerosis Type 6

  2009cited by this paper
• Bridging high-throughput genetic and transcriptional data reveals cellular responses to alpha-synuclein toxicity

  2009cited by this paper
• Compositional Determinants of Prion Formation in Yeast

  2009cited by this paper
• Mutations in the FUS/TLS Gene on Chromosome 16 Cause Familial Amyotrophic Lateral Sclerosis

  2009cited by this paper
• Abundant FUS-immunoreactive pathology in neuronal intermediate filament inclusion disease

  2009cited by this paper
• TDP‐43 is recruited to stress granules in conditions of oxidative insult

  2009cited by this paper
• A systematic survey identifies prions and illuminates sequence features of prionogenic proteins.

  2009cited by this paper
• Eukaryotic stress granules: the ins and outs of translation.

  2009cited by this paper
• TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis

  2008cited by this paper
• A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity

  2008influential reference
• P bodies promote stress granule assembly in Saccharomyces cerevisiae

  2008cited by this paper
• Structural determinants of the cellular localization and shuttling of TDP-43

  2008cited by this paper
• Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity.

  2008cited by this paper
• RNA-binding Protein TLS Is a Major Nuclear Aggregate-interacting Protein in Huntingtin Exon 1 with Expanded Polyglutamine-expressing Cells*

  2008cited by this paper
• Misfolded proteins partition between two distinct quality control compartments

  2008influential reference
• Ataxin-2 interacts with the DEAD/H-box RNA helicase DDX6 and interferes with P-bodies and stress granules.

  2007cited by this paper
• alpha-Synuclein budding yeast model: toxicity enhanced by impaired proteasome and oxidative stress.

  2006cited by this paper
• Purification and analysis of prion and amyloid aggregates.

  2006influential reference
• Faculty Opinions recommendation of Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models.

  2006cited by this paper
• How to find a prion: [URE3], [PSI+] and [beta].

  2006cited by this paper
• α-Synuclein Blocks ER-Golgi Traffic and Rab1 Rescues Neuron Loss in Parkinson's Models

  2006cited by this paper
• Nonsense Suppression in Yeast Cells Overproducing Sup35 (eRF3) Is Caused by Its Non-heritable Amyloids*

  2005cited by this paper
• Domain Architectures and Characterization of an RNA-binding Protein, TLS*

  2004cited by this paper
• Aggregation of Expanded Polyglutamine Domain in Yeast Leads to Defects in Endocytosis

  2003cited by this paper
• Yeast Cells Provide Insight into Alpha-Synuclein Biology and Pathobiology

  2003cited by this paper
• Yeast [PSI+] Prion Aggregates Are Formed by Small Sup35 Polymers Fragmented by Hsp104*

  2003cited by this paper
• Huntingtin toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1

  2002influential reference
• Prion Filament Networks in [Ure3] Cells of Saccharomyces cerevisiae

  2001cited by this paper
• Prion properties of the Sup35 protein of yeast Pichia methanolica

  2000cited by this paper
• Evolutionary conservation of prion‐forming abilities of the yeast Sup35 protein

  2000cited by this paper
• Molecular basis of a yeast prion species barrier.

  2000cited by this paper
• Nucleated conformational conversion and the replication of conformational information by a prion determinant.

  2000cited by this paper
• Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins.

  2000influential reference
• Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils.

  2000influential reference
• TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling.

  1997cited by this paper
• Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+].

  1995cited by this paper
• Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis

  1993cited by this paper
• Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis.

  1993cited by this paper

• FUS and TDP-43 aggregation are uncoupled from toxicity in ageing yeast models.

  2026cites this paper
• Recent Advances in Co-Condensation and Co-Aggregation of Amyloid Proteins Linked to Neurodegenerative Diseases.

  2025cites this paper
• A Twist in Yeast: New Perspectives for Studying TDP-43 Proteinopathies in S. cerevisiae

  2025cites this paper
• From Yeast to Therapeutics: Modeling Neurodegenerative Diseases in Saccharomyces cerevisiae

  2025cites this paper
• Technologies for studying phase-separated biomolecular condensates

  2024cites this paper
• The prion-like effect and prion-like protein targeting strategy in amyotrophic lateral sclerosis

  2024cites this paper
• RNA and the RNA-binding protein FUS act in concert to prevent TDP-43 spatial segregation

  2024cites this paper
• Expression of Wild-Type and Mutant Human TDP-43 in Yeast Inhibits TOROID (TORC1 Organized in Inhibited Domain) Formation and Autophagy Proportionally to the Levels of TDP-43 Toxicity

  2024cites this paper
• RNA and FUS act in concert to prevent TDP-43 spatial segregation

  2023cites this paper
• The implications of physiological biomolecular condensates in amyotrophic lateral sclerosis.

  2023cites this paper
• Structural Integrity of Nucleolin Is Required to Suppress TDP-43-Mediated Cytotoxicity in Yeast and Human Cell Models

  2023cites this paper
• Differential roles for DNAJ isoforms in HTT-polyQ and FUS aggregation modulation revealed by chaperone screens

  2022cites this paper
• [PRION+] States Are Associated with Specific Histone H3 Post-Translational Modification Changes

  2022cites this paper
• Phase separation of FG-nucleoporins in nuclear pore complexes.

  2022cites this paper
• TDP-43 Toxicity in Yeast Is Associated with a Reduction in Autophagy, and Deletions of TIP41 and PBP1 Counteract These Effects

  2022cites this paper
• Differential roles for DNAJ isoforms in HTT-polyQ and mutant FUS aggregation modulation revealed by chaperone network screens

  2021cites this paper
• Trends in Understanding the Pathological Roles of TDP-43 and FUS Proteins.

  2021cites this paper
• Genetic architecture of motor neuron diseases.

  2021cites this paper
• Huntingtin Polyglutamine Fragments Are a Substrate for Hsp104 in Saccharomyces cerevisiae

  2021cites this paper
• Wild-Type and Mutant FUS Expression Reduce Proliferation and Neuronal Differentiation Properties of Neural Stem Progenitor Cells

  2021cites this paper
• A yeast model of the ALS protein Matrin3 uncovers Hsp90 and its co-chaperone Sti1 as modifiers of misfolding and toxicity

  2021cites this paper
• The prion-like domain of Fused in Sarcoma is phosphorylated by multiple kinases affecting liquid- and solid-phase transitions

  2020cites this paper
• The FUS gene is dual‐coding with both proteins contributing to FUS‐mediated toxicity

  2020cites this paper
• Application of yeast to studying amyloid and prion diseases.

  2020cites this paper
• Connecting RNA-Modifying Similarities of TDP-43, FUS, and SOD1 with MicroRNA Dysregulation Amidst A Renewed Network Perspective of Amyotrophic Lateral Sclerosis Proteinopathy

  2020cites this paper
• Molecular interactions underlying liquid-liquid phase separation of the FUS low complexity domain

  2019cites this paper
• Amyloid-Forming Segment Induces Aggregation of FUS-LC Domain from Phase Separation Modulated by Site-Specific Phosphorylation.

  2019cites this paper
• FUS gene is dual-coding with both proteins united in molecular hallmarks of amyotrophic lateral sclerosis

  2019cites this paper
• Proteome-Scale Mapping of Perturbed Proteostasis in Living Cells.

  2019cites this paper
• Identifying Anti-prion Chemical Compounds Using a Newly Established Yeast High-Throughput Screening System.

  2019cites this paper
• Fused in Sarcoma: Properties, Self-Assembly and Correlation with Neurodegenerative Diseases

  2019cites this paper
• Molecular interactions underlying liquid-liquid phase separation of the FUS low complexity domain

  2019cites this paper
• Calcium-responsive transactivator (CREST) toxicity is rescued by loss of PBP1/ATXN2 function in a novel yeast proteinopathy model and in transgenic flies

  2019cites this paper
• FUS gene is dual-coding with both proteins united in FUS-mediated toxicity

  2019cites this paper
• The debated toxic role of aggregated TDP-43 in amyotrophic lateral sclerosis: a resolution in sight?

  2019cites this paper
• Studying Spatial Protein Quality Control, Proteopathies, and Aging Using Different Model Misfolding Proteins in S. cerevisiae

  2018cites this paper
• Yeast Models of Prion-Like Proteins That Cause Amyotrophic Lateral Sclerosis Reveal Pathogenic Mechanisms

  2018cites this paper
• The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS

  2018cites this paper
• A yeast model of calcium-responsive transactivator protein (CREST) proteinopathy shows that PBP1/ATXN2 modifies CREST aggregation and toxicity

  2018cites this paper
• The prionlike domain of FUS is multiphosphorylated following DNA damage without altering nuclear localization

  2018cites this paper
• Yeast as a model to study protein misfolding in aged cells.

  2018cites this paper
• Yeast as a Model to Unravel Mechanisms Behind FUS Toxicity in Amyotrophic Lateral Sclerosis

  2018influential citation
• The Insoluble Protein Deposit (IPOD) in Yeast

  2018cites this paper
• ALS Yeast Models—Past Success Stories and New Opportunities

  2018cites this paper
• FUS toxicity is rescued by the modulation of lncRNA hsrω expression in Drosophila melanogaster

  2017cites this paper
• PINK1 and Parkin are genetic modifiers for FUS-induced neurodegeneration

  2017cites this paper
• Phosphorylation of the FUS low‐complexity domain disrupts phase separation, aggregation, and toxicity

  2017influential citation
• Overexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis

  2017cites this paper
• The FUS protein: Physiological functions and a role in amyotrophic lateral sclerosis

  2017cites this paper
• Altered mRNP granule dynamics in FTLD pathogenesis

  2016cites this paper
• Stress granules at the intersection of autophagy and ALS.

  2016cites this paper
• Parkin Misfolding, Dysfunction, and Degradation in Parkinson's Disease

  2016cites this paper
• Development of a chick embryo model to study important regulatory domains of human genes implicated in Motor Neurone Disease

  2016cites this paper
• Hunting for huntingtin associated factors: Identification and characterization of huntingtin expanded polyglutamine aggregate associated factors and their impact on Huntington disease model cellular toxicity

  2016cites this paper
• PINK1 and Parkin are genetic modifiers for FUS-induced neurodegeneration.

  2016cites this paper
• Physiological functions and pathobiology of TDP‐43 and FUS/TLS proteins

  2016cites this paper
• FUS Interacts with HSP60 to Promote Mitochondrial Damage

  2015cites this paper
• Structural modifications of the RNA-binding protein, fused in sarcoma : implications for amyotrophic lateral sclerosis

  2015cites this paper
• Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates

  2015cites this paper
• Ubiquitin-dependent proteolysis in yeast cells expressing neurotoxic proteins

  2015cites this paper
• The oncofusion protein FUS–ERG targets key hematopoietic regulators and modulates the all-trans retinoic acid signaling pathway in t(16;21) acute myeloid leukemia

  2015cites this paper
• Characterisation of multiple regulatory domains spanning the major transcriptional start site of the FUS gene, a candidate gene for motor neurone disease.

  2015cites this paper
• Regulatory chaperone complexes in neurodegenerative diseases: a perspective on therapeutic intervention.

  2014cites this paper
• The role of FUS gene variants in neurodegenerative diseases

  2014cites this paper
• Yeast models for amyloid disease.

  2014cites this paper
• Characterization of De Novo Aggregation of Prions and Protein Misfolding Disease Proteins in Yeast

  2014cites this paper
• Chaperone-dependent Neurodegeneration: A Molecular Perspective on Therapeutic Intervention

  2013cites this paper
• Identification of Genetic Modifiers of TDP-43 Neurotoxicity in Drosophila

  2013cites this paper
• Harnessing the power of yeast to unravel the molecular basis of neurodegeneration

  2013influential citation
• RNA-binding ability of FUS regulates neurodegeneration, cytoplasmic mislocalization and incorporation into stress granules associated with FUS carrying ALS-linked mutations.

  2013cites this paper
• Fused in sarcoma (FUS): an oncogene goes awry in neurodegeneration.

  2013cites this paper
• Characterization of FUS Mutations in Amyotrophic Lateral Sclerosis Using RNA-Seq

  2013cites this paper
• Amyotrophic lateral sclerosis: new insights into underlying molecular mechanisms and opportunities for therapeutic intervention.

  2012cites this paper
• TDP-43 and FUS RNA-binding Proteins Bind Distinct Sets of Cytoplasmic Messenger RNAs and Differently Regulate Their Post-transcriptional Fate in Motoneuron-like Cells*

  2012cites this paper
• A yeast model of optineurin proteinopathy reveals a unique aggregation pattern associated with cellular toxicity

  2012cites this paper
• RNA‐binding proteins in neurodegenerative disease: TDP‐43 and beyond

  2012cites this paper
• Genetics of Familial Amyotrophic Lateral Sclerosis

  2012cites this paper
• FUS-related proteinopathies: lessons from animal models.

  2012cites this paper
• Complexity of familial amyotrophic lateral sclerosis

  2012cites this paper
• Evaluating the role of the FUS/TLS-related gene EWSR1 in amyotrophic lateral sclerosis.

  2012cites this paper
• Mechanizmy patogenetyczne stwardnienia bocznego zanikowego

  2012cites this paper
• Endogenous TDP-43, but not FUS, contributes to stress granule assembly via G3BP

  2012cites this paper
• Mitochondrion-mediated cell death: dissecting yeast apoptosis for a better understanding of neurodegeneration

  2012cites this paper
• Neurodegeneration the RNA way.

  2012cites this paper
• RNA-Binding Proteins in Amyotrophic Lateral Sclerosis and Neurodegeneration

  2012cites this paper
• The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease.

  2012cites this paper
• Motor neuron apoptosis and neuromuscular junction perturbation are prominent features in a Drosophila model of Fus-mediated ALS

  2012cites this paper
• Using yeast models to probe the molecular basis of amyotrophic lateral sclerosis.

  2011cites this paper
• Modeling ALS and FTLD proteinopathies in yeast: An efficient approach for studying protein aggregation and toxicity

  2011cites this paper
• Yeast as a Model for Studying A Aggregation, Toxicity and Clearance

  2011cites this paper
• TDP-43 and FUS: a nuclear affair.

  2011cites this paper
• RNA-binding proteins with prion-like domains in ALS and FTLD-U

  2011cites this paper
• [ ( Figure _ 1 ) TD $ FIG ]

  2011cites this paper
• FUS and TARDBP but Not SOD1 Interact in Genetic Models of Amyotrophic Lateral Sclerosis

  2011cites this paper
• Site-specific structural analysis of a yeast prion strain with species-specific seeding activity

  2011cites this paper
• Modeling Huntington disease in yeast: Perspectives and future directions

  2011cites this paper
• Motor neuron, nerve, and neuromuscular junction disease.

  2011cites this paper
• Protein misfolding and aggregation : a common feature among neurodegenerative diseases

  year unknowncites this paper