Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis

Ling, Shuo-Chien; Polymenidou, Magdalini; Cleveland, Don W.

doi:10.1016/j.neuron.2013.07.033

Cited by 1,811Amyotrophic Lateral Sclerosis ResearchAlzheimer's disease research and treatmentsGenetic Neurodegenerative Diseases

Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis

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Ling, Shuo-Chien, Polymenidou, Magdalini, Cleveland, Don W.·2013·Neuron

DOI 10.1016/j.neuron.2013.07.033PMC PMC4411085

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Abstract

Breakthrough discoveries identifying common genetic causes for amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD) have transformed our view of these disorders. They share unexpectedly similar signatures, including dysregulation in common molecular players including TDP-43, FUS/TLS, ubiquilin-2, VCP, and expanded hexanucleotide repeats within the C9ORF72 gene. Dysfunction in RNA processing and protein homeostasis is an emerging theme. We present the case here that these two processes are intimately linked, with disease-initiated perturbation of either leading to further deviation of both protein and RNA homeostasis through a feedforward loop including cell-to-cell prion-like spread that may represent the mechanism for relentless disease progression.

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ALS is a disease of the spinal cord in which astrocytes, microglia, and oligodendrocytes all contribute to disease progression.
“Rather, it is a disease of the spinal cord in which astrocytes, microglia, and oligodendrocytes all contribute to disease progression (Ling et al., 2013).”
From An RNA-Sequencing Transcriptome and Splicing Database of Glia, Neurons, and Vascular Cells of the Cerebral Cortex (2014) · cites this paper as Ling et al., 2013
The Introduction (page unavailable) describes ALS as involving both lower motor neurons and upper motor neurons with their corticospinal tracts, so calling it solely a disease of the spinal cord is too narrow. The “SOD1: a central component of ALS or an outlier?” section (page unavailable) identifies astrocytes and microglia as determinants of accelerated progression in mutant-SOD1 mouse models, but links oligodendrocyte precursors to disease onset, not progression. The claim extends those model-specific findings to ALS generally. (LLM, conf=0.88)
Experimental — accuracy not yet measured
The majority of disease-associated FUS mutations affect the C-terminal nuclear localization signal, resulting in cytosolic mislocalization and aggregation of mutant FUS.
“The majority of disease-associated FUS mutations affect the C-terminal nuclear localization signal, resulting in cytosolic mislocalization and aggregation of mutant FUS [232–234].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [234]
Dysfunction of TDP43 and FUS leads to phenotypes characteristic of ALS and FTLD.
“Dysfunction of transactivating response DNA binding protein (TDP43; also known as TARDBP) and fused in sarcoma (FUS; also known as TLS) lead to phenotypes that are characteristic of amyotrophic lateral sclerosis (ALS) and frontal temporal lobar disease (FTLD)”
From The neurogenetics of alternative splicing (2016) · cites this paper as [156]
TDP43 is a major component of cytoplasmic inclusions found in 95% of cases of sporadic ALS and FTLD.
“TDP43 is a major component of cytoplasmic inclusions found in 95% cases of sporadic ALS and FTLD156.”
From The neurogenetics of alternative splicing (2016) · cites this paper as [156]

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RNA Gain-of-Function in Spinocerebellar Ataxia Type 8
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Widespread binding of FUS along nascent RNA regulates alternative splicing in the brain
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Requirements for Stress Granule Recruitment of Fused in Sarcoma (FUS) and TAR DNA-binding Protein of 43 kDa (TDP-43)
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Intermolecular transmission of superoxide dismutase 1 misfolding in living cells
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The TET Family of Proteins: Functions and Roles in Disease
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The clinical and pathological phenotype of C9ORF72 hexanucleotide repeat expansions
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Pathological hallmarks of amyotrophic lateral sclerosis/frontotemporal lobar degeneration in transgenic mice produced with TDP-43 genomic fragments
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TARDBP and FUS Mutations Associated with Amyotrophic Lateral Sclerosis: Summary and Update
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Mutations in CHMP2B in Lower Motor Neuron Predominant Amyotrophic Lateral Sclerosis (ALS)
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Chromosome 9p21 in amyotrophic lateral sclerosis in Finland: a genome-wide association study
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FUS-SMN Protein Interactions Link the Motor Neuron Diseases ALS and SMA
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TDP-43 Mediates Degeneration in a Novel Drosophila Model of Disease Caused by Mutations in VCP/p97
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TDP‐43, a neuro‐pathosignature factor, is essential for early mouse embryogenesis
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Motor Neuron Disease-Associated Mutant Vesicle-Associated Membrane Protein-Associated Protein (VAP) B Recruits Wild-Type VAPs into Endoplasmic Reticulum-Derived Tubular Aggregates
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Discovery of Novel DENN Proteins: Implications for the Evolution of Eukaryotic Intracellular Membrane Structures and Human Disease
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Male sterility and enhanced radiation sensitivity in TLS−/− mice
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The Amyotrophic Lateral Sclerosis 8 Protein VAPB Is Cleaved, Secreted, and Acts as a Ligand for Eph Receptors
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Mutation within TARDBP leads to Frontotemporal Dementia without motor neuron disease
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Mutations in SQSTM1 encoding p62 in amyotrophic lateral sclerosis: genetics and neuropathology
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Nuclear factor TDP‐43 can affect selected microRNA levels
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p62: a versatile multitasker takes on cancer
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Familial amyotrophic lateral sclerosis
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A Seeding Reaction Recapitulates Intracellular Formation of Sarkosyl-insoluble Transactivation Response Element (TAR) DNA-binding Protein-43 Inclusions*♦
Furukawa, Y., Kaneko, K., Watanabe, S., Yamanaka, K., & Nukina, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.231209 · Cited by 235 · see citing works
Chromosome 9p21 in sporadic amyotrophic lateral sclerosis in the UK and seven other countries: a genome-wide association study
Shatunov, A., Mok, K. Y., Newhouse, S., Weale, M. E., Smith, B. N., Vance, C. A., Johnson, L., Veldink, J. H., van Es, M. A., van den Berg, L. H., et al. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70197-6 · Cited by 231 · see citing works
Initiation and elongation in fibrillation of ALS-linked superoxide dismutase
Chattopadhyay, M., Durazo, A., Sohn, S. H., Strong, C. D., Gralla, E. B., Whitelegge, J. P., & Valentine, J. S. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807058105 · Cited by 228 · see citing works
Clinical and pathological features of familial frontotemporal dementia caused by C9ORF72 mutation on chromosome 9p
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Position-dependent FUS-RNA interactions regulate alternative splicing events and transcriptions
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Characterization of Amyotrophic Lateral Sclerosis-linked P56S Mutation of Vesicle-associated Membrane Protein-associated Protein B (VAPB/ALS8)
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Regulation of TDP-43 aggregation by phosphorylation andp62/SQSTM1: Regulation of TDP-43 aggregation by phosphorylation and p62
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Nuclear localization sequence of FUS and induction of stress granules by ALS mutants
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TDP-43 aggregation in neurodegeneration: Are stress granules the key?
Dewey, C. M., Cenik, B., Sephton, C. F., Johnson, B. A., Herz, J., & Yu, G. (2012) · Brain Research · doi:10.1016/j.brainres.2012.02.032 · Cited by 211 · see citing works
Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system
Wang, X., Fan, H., Ying, Z., Li, B., Wang, H., & Wang, G. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2009.11.055 · Cited by 207 · see citing works
Clinical characteristics of patients with familial amyotrophic lateral sclerosis carrying the pathogenic GGGGCC hexanucleotide repeat expansion of C9ORF72
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Spliceosome integrity is defective in the motor neuron diseases ALS and SMA
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FUS Transgenic Rats Develop the Phenotypes of Amyotrophic Lateral Sclerosis and Frontotemporal Lobar Degeneration
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Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form
Kerman, A., Liu, H., Croul, S. E., Bilbao, J. M., Rogaeva, E. A., Zinman, L. H., Robertson, J., & Chakrabartty, A. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0646-5 · Cited by 205 · see citing works
Autoregulation of TDP-43 mRNA levels involves interplay between transcription, splicing, and alternative polyA site selectionPreprint
Avendaño-Vázquez, S. E., Dhir, A., Bembich, S., Buratti, E., Proudfoot, N. J., & Baralle, F. E. (2012) · Genes & Development · doi:10.1101/gad.194829.112 · Cited by 205 · see citing works
Juvenile ALS with basophilic inclusions is a FUS proteinopathy with FUS mutations
Bäumer, D., Hilton, D. A., Paine, S., Turner, M. R., Lowe, J. S., Talbot, K., & Ansorge, O. (2010) · Neurology · doi:10.1212/wnl.0b013e3181ed9cde · Cited by 202 · see citing works
Transgenic Rat Model of Neurodegeneration Caused by Mutation in the TDP Gene
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TARDBP variation associated with frontotemporal dementia, supranuclear gaze palsy, and chorea
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Expression of ALS‐linked TDP‐43 mutant in astrocytes causes non‐cell‐autonomous motor neuron death in rats
Tong, J., Huang, C., Bi, F., Wu, Q., Huang, B., Liu, X., Li, F., Zhou, H., & Xia, X. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.122 · Cited by 196 · see citing works
TDP-43: gumming up neurons through protein–protein and protein–RNA interactions
Buratti, E., & Baralle, F. E. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.03.003 · Cited by 195 · see citing works
Loss of TDP-43 causes age-dependent progressive motor neuron degeneration
Iguchi, Y., Katsuno, M., Niwa, J.-I., Takagi, S., Ishigaki, S., Ikenaka, K., Kawai, K., Watanabe, H., Yamanaka, K., Takahashi, R., et al. (2013) · Brain · doi:10.1093/brain/awt029 · Cited by 195 · see citing works
The molecular basis of the frontotemporal lobar degeneration–amyotrophic lateral sclerosis spectrum
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Disruption of endocytic trafficking in frontotemporal dementia with CHMP2B mutations
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Characterization of the Properties of a Novel Mutation in VAPB in Familial Amyotrophic Lateral Sclerosis
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Prion-like spread of protein aggregates in neurodegeneration
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Self-citation
Pathological heterogeneity in amyotrophic lateral sclerosis with FUS mutations: two distinct patterns correlating with disease severity and mutation
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Pattern of ubiquilin pathology in ALS and FTLD indicates presence of C9ORF72 hexanucleotide expansion
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Aberrant Localization of FUS and TDP43 Is Associated with Misfolding of SOD1 in Amyotrophic Lateral Sclerosis
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Phenotype difference between ALS patients with expanded repeats in C9ORF72 and patients with mutations in other ALS-related genes
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Intercellular (Mis)communication in Neurodegenerative Disease
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Misregulated RNA processing in amyotrophic lateral sclerosis
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Self-citation
Nuclear transport impairment of amyotrophic lateral sclerosis‐linked mutations in FUS/TLS
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An RNA-Sequencing Transcriptome and Splicing Database of Glia, Neurons, and Vascular Cells of the Cerebral Cortex
Zhang, Y., Chen, K., Sloan, S. A., Bennett, M. L., Scholze, A. R., O'Keeffe, S., Phatnani, H. P., Guarnieri, P., Caneda, C., Ruderisch, N., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.1860-14.2014 · Cited by 4,875 · see citing works
“Rather, it is a disease of the spinal cord in which astrocytes, microglia, and oligodendrocytes all contribute to disease progression (Ling et al., 2013).”
Background
Hallmarks of neurodegenerative diseases
Wilson, D. M., Cookson, M. R., Van Den Bosch, L., Zetterberg, H., Holtzman, D. M., & Dewachter, I. (2023) · Cell · doi:10.1016/j.cell.2022.12.032 · Cited by 1,789 · see citing works
Principles and Properties of Stress Granules
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Alternative polyadenylation of mRNA precursors
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RNA mis-splicing in disease
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Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II
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ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain
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Antisense oligonucleotides: the next frontier for treatment of neurological disorders
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Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis
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C9orf72-mediated ALS and FTD: multiple pathways to disease
Balendra, R., & Isaacs, A. M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0047-2 · Cited by 715 · see citing works
TDP-43 repression of nonconserved cryptic exons is compromised in ALS-FTD
Ling, J. P., Pletniková, O., Troncoso, J. C., & Wong, P. C. (2015) · Science · doi:10.1126/science.aab0983 · Cited by 673 · see citing works
ALS-implicated protein TDP-43 sustains levels of STMN2, a mediator of motor neuron growth and repair
Klim, J. R., Williams, L. A., Limone, F., Guerra San Juan, I., Davis-Dusenbery, B. N., Mordes, D. A., Burberry, A., Steinbaugh, M. J., Gamage, K. K., Kirchner, R., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0300-4 · Cited by 653 · see citing works
Phase Separation of FUS Is Suppressed by Its Nuclear Import Receptor and Arginine Methylation
Hofweber, M., Hutten, S., Bourgeois, B. M. R., Spreitzer, E., Niedner, A., Schifferer, M., Ruepp, M., Simons, M., Niessing, D., Madl, T., et al. (2018) · Cell · doi:10.1016/j.cell.2018.03.004 · Cited by 654 · see citing works
Premature polyadenylation-mediated loss of stathmin-2 is a hallmark of TDP-43-dependent neurodegeneration
Melamed, Z., López-Erauskin, J., Baughn, M. W., Zhang, O., Drenner, K., Sun, Y., Freyermuth, F., McMahon, M. A., Beccari, M. S., Artates, J. W., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0293-z · Cited by 635 · see citing works
Self-citation
Preclinical research: Make mouse studies work
Perrin, S. (2014) · Nature · doi:10.1038/507423a · Cited by 668 · see citing works
TDP-43 pathology disrupts nuclear pore complexes and nucleocytoplasmic transport in ALS/FTD
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Gruijs da Silva, L. A., Simonetti, F., Hutten, S., Riemenschneider, H., Sternburg, E. L., Pietrek, L. M., Gebel, J., Dötsch, V., Edbauer, D., Hummer, G., et al. (2022) · The EMBO Journal · doi:10.15252/embj.2021108443 · Cited by 192 · see citing works
Mitochondria Associated Membranes (MAMs): Architecture and physiopathological role
Barazzuol, L., Giamogante, F., & Calí, T. (2021) · Cell Calcium · doi:10.1016/j.ceca.2020.102343 · Cited by 202 · see citing works

RNA Dysfunction and RNA binding Proteins in the Syndrome of ALS/FTD
(2013) · Journal of Syndromes · doi:10.13188/2380-6036.1000002
Defects in RNA Metabolism links FTD and ALS Pathogenesis: TDP-43, FUS, and C9orf72
Deng, Q., Chalermpalanupap, T., & Kukar, T. L. (2013) · Current Enzyme Inhibition · doi:10.2174/1573408011309010005 · Cited by 1 · see citing works
Misregulated RNA processing in amyotrophic lateral sclerosis
Polymenidou, M., Lagier-Tourenne, C., Hutt, K. R., Bennett, C. F., Cleveland, D. W., & Yeo, G. W. (2012) · Brain Research · doi:10.1016/j.brainres.2012.02.059 · Cited by 169 · see citing works
Self-citation
Biological Spectrum of Amyotrophic Lateral Sclerosis PrionsPreprint
Polymenidou, M., & Cleveland, D. W. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024133 · Cited by 28 · see citing works
Self-citation
RNA-binding proteins in ALS and FTD: from pathogenic mechanisms to therapeutic insights
Rummens, J., & Cruz, S. D. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00851-y · Cited by 52 · see citing works

Authors: Ling, S.-C., Polymenidou, M., & Cleveland, D. W.
Affiliations: University of California San Diego (US)
Corresponding author: Cleveland, Don W.
ORCID: Ling, Shuo-Chien
Polymenidou, Magdalini
Cleveland, Don W.
Venue: Neuron
Publisher: Elsevier BV
Published: 2013-08
Volume: 79
Issue: 3
Pages: 416-438
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/j.neuron.2013.07.033
PMC: PMC4411085
OpenAlex: W2073073462
Cited by: 1,811
References: 260
Citations by year: 2026: 124 · 2025: 156 · 2024: 149 · 2023: 166 · 2022: 137 · 2021: 170 · 2020: 175 · 2019: 129 · 2018: 139 · 2017: 130 · 2016: 126 · 2015: 98 · 2014: 99 · 2013: 12
FWCI: 14.56
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 371 d)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: Neuron (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
eScholarship (California Digital Library) (submittedVersion)
Funders: Ludwig Institute for Cancer Research
National Institutes of Health (K99-NS075216, R01-NS27036)
National Institute on Aging (T32 AG 000216)
Topics: Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
Keywords: amyotrophic lateral sclerosis, frontotemporal dementia, RNA homeostasis, proteostasis, TDP-43, FUS/TLS, UBQLN2, VCP, C9orf72 repeat expansion, RNA processing, prion-like spread, feed-forward loop, disease progression
MeSH terms: Autophagy-Related Proteins, C9orf72 Protein, Valosin Containing Protein, Adenosine Triphosphatases, Amyotrophic Lateral Sclerosis, Animals, DNA-Binding Proteins, Homeostasis, Humans, Models, Biological, Mutation, Proteins, RNA, Ubiquitins, Cell Cycle Proteins, RNA-Binding Protein FUS, Adaptor Proteins, Signal Transducing, Frontotemporal Dementia

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Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis

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