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Opposing roles of p38α-mediated phosphorylation and arginine methylation in driving TDP-43 proteinopathy

https://doi.org/10.1101/2021.08.04.455154

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Phosphorylated TDP‐43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

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CDC7 inhibition blocks pathological TDP‐43 phosphorylation and neurodegeneration

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Proteomics: the move to mixtures

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The clinical trial landscape in amyotrophic lateral sclerosis—Past, present, and future

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Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies

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TARDBP 3′-UTR variant in autopsy-confirmed frontotemporal lobar degeneration with TDP-43 proteinopathy

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An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database

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The physical forces mediating self-association and phase-separation in the C-terminal domain of TDP-43

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TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

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Identification of casein kinase-1 phosphorylation sites on TDP-43

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Identification of the methylation preference region in heterogeneous nuclear ribonucleoprotein K by protein arginine methyltransferase 1 and its implication in regulating nuclear/cytoplasmic distribution

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The N-terminus of TDP-43 promotes its oligomerization and enhances DNA binding affinity

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A phosphomimetic mutant TDP-43 (S409/410E) induces Drosha instability and cytotoxicity in Neuro 2A cells

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Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization

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FUS Phase Separation Is Modulated by a Molecular Chaperone and Methylation of Arginine Cation-π Interactions

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Age-Dependent TDP-43-Mediated Motor Neuron Degeneration Requires GSK3, hat-trick, and xmas-2

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Serine phosphorylation and arginine methylation at the crossroads to neurodegeneration

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Phosphorylated and ubiquitinated TDP‐43 pathological inclusions in ALS and FTLD‐U are recapitulated in SH‐SY5Y cells

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Methylarginines within the RGG-Motif Region of hnRNP A1 Affect Its IRES Trans-Acting Factor Activity and Are Required for hnRNP A1 Stress Granule Localization and Formation

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Arginine Methylation of FOXO Transcription Factors Inhibits Their Phosphorylation by Akt

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Defining the RGG/RG Motif

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Poly(ADP-Ribose) Prevents Pathological Phase Separation of TDP-43 by Promoting Liquid Demixing and Stress Granule Localization

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p38 MAP kinase: a convergence point in cancer therapy

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Inhibition of p38 mitogen activated protein kinase activation and mutant SOD1G93A-induced motor neuron death

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Screening of the TARDBP gene in familial and sporadic amyotrophic lateral sclerosis patients of Chinese origin

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Screening of a neuronal cell model of tau pathology for therapeutic compounds

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Axonal Transport of TDP-43 mRNA Granules Is Impaired by ALS-Causing Mutations

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RNA Binding Antagonizes Neurotoxic Phase Transitions of TDP-43

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Cytoplasmic TDP-43 De-mixing Independent of Stress Granules Drives Inhibition of Nuclear Import, Loss of Nuclear TDP-43, and Cell Death

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Nucleocytoplasmic Proteomic Analysis Uncovers eRF1 and Nonsense-Mediated Decay as Modifiers of ALS/FTD C9orf72 Toxicity

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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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FUS and TDP-43 Phases in Health and Disease

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ALS Genes in the Genomic Era and their Implications for FTD

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Persistent activation of p38 mitogen-activated protein kinase in a mouse model of familial amyotrophic lateral sclerosis correlates with disease progression

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Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels

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Discovery of 6-(2,4-Difluorophenoxy)-2-[3-hydroxy-1-(2-hydroxyethyl)propylamino]-8-methyl-8 H -pyrido[2,3- d ]pyrimidin-7-one (Pamapimod) and 6-(2,4-Difluorophenoxy)-8-methyl-2-(tetrahydro-2 H -pyran-4-ylamino)pyrido[2,3- d ]pyrimidin-7(8 H )-one (R1487) as Orally Bioavailable and Highly Selective…

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Global Analysis of TDP-43 Interacting Proteins Reveals Strong Association with RNA Splicing and Translation Machinery

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Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation negatively modulates EGFR-mediated ERK activation

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Methylation of FEN1 suppresses nearby phosphorylation and facilitates PCNA binding

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Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43

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The N-terminal dimerization is required for TDP-43 splicing activity

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TDP-43 regulation of stress granule dynamics in neurodegenerative disease-relevant cell types

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The Clinical Trial

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ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS

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ALS-linked TDP-43 mutations produce aberrant RNA splicing and adult-onset motor neuron disease without aggregation or loss of nuclear TDP-43

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PRMT1 Is the Predominant Type I Protein Arginine Methyltransferase in Mammalian Cells

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Chronic oxidative stress promotes GADD34-mediated phosphorylation of the TAR DNA-binding protein TDP-43, a modification linked to neurodegeneration

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Active Mutants of the Human p38α Mitogen-activated Protein Kinase

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TDP-43 Binds Heterogeneous Nuclear Ribonucleoprotein A/B through Its C-terminal Tail

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Disturbance of Nuclear and Cytoplasmic TAR DNA-binding Protein (TDP-43) Induces Disease-like Redistribution, Sequestration, and Aggregate Formation

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Immunoaffinity Enrichment and Mass Spectrometry Analysis of Protein Methylation

inferredcites →https://doi.org/10.1080/14728222.2018.1439923openalex-snapshot

TDP-43 post-translational modifications in health and disease

inferredcites →https://doi.org/10.1080/15384101.2015.1033595openalex-snapshot

PRMT5- mediated symmetric arginine dimethylation is attenuated by mutant huntingtin and is impaired in Huntington's disease (HD)

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inferredcites →https://doi.org/10.1093/emboj/18.18.4969openalex-snapshot

The p38 MAP kinase pathway signals for cytokine‐induced mRNA stabilization via MAP kinase‐activated protein kinase 2 and an AU‐rich region‐targeted mechanism

inferredcites →https://doi.org/10.1093/hmg/ddr021openalex-snapshot

TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1

inferredcites →https://doi.org/10.1093/hmg/ddt498openalex-snapshot

TDP-43 Phosphorylation by casein kinase Iε promotes oligomerization and enhances toxicity in vivo

inferredcites →https://doi.org/10.1093/hmg/ddu493openalex-snapshot

Opposing roles of p38 and JNK in a Drosophila model of TDP-43 proteinopathy reveal oxidative stress and innate immunity as pathogenic components of neurodegeneration

inferredcites →https://doi.org/10.1093/hmg/ddu497openalex-snapshot

Activation of AMP-activated protein kinase α1 mediates mislocalization of TDP-43 in amyotrophic lateral sclerosis

inferredcites →https://doi.org/10.1093/jnen/63.2.113openalex-snapshot

Activated p38MAPK Is a Novel Component of the Intracellular Inclusions Found in Human Amyotrophic Lateral Sclerosis and Mutant SOD1 Transgenic Mice

inferredcites →https://doi.org/10.1093/nar/gky103openalex-snapshot

Arginine methylation of the C-terminus RGG motif promotes TOP3B topoisomerase activity and stress granule localization

inferredcites →https://doi.org/10.1101/cshperspect.a011254openalex-snapshot

MAP Kinase Pathways

inferredcites →https://doi.org/10.1101/cshperspect.a024554openalex-snapshot

Biology and Pathobiology of TDP-43 and Emergent Therapeutic Strategies

inferredcites →https://doi.org/10.1111/j.1471-4159.2010.07098.xopenalex-snapshot

Regulation of TDP-43 aggregation by phosphorylation andp62/SQSTM1

inferredcites →https://doi.org/10.1126/science.1134108openalex-snapshot

Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

inferredcites →https://doi.org/10.1126/science.1154584openalex-snapshot

TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis

inferredcites →https://doi.org/10.1126/scisignal.aaf7329openalex-snapshot

Proteome-wide analysis of arginine monomethylation reveals widespread occurrence in human cells

inferredcites →https://doi.org/10.1126/scitranslmed.abb3774openalex-snapshot

C9orf72 poly(GR) aggregation induces TDP-43 proteinopathy

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The Role of p38 MAPK and Its Substrates in Neuronal Plasticity and Neurodegenerative Disease

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Methylation of C/EBPα by PRMT1 Inhibits Its Tumor-Suppressive Function in Breast Cancer

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p38 MAPKs — roles in skeletal muscle physiology, disease mechanisms, and as potential therapeutic targets

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Association between novel TARDBP mutations and Chinese patients with amyotrophic lateral sclerosis

inferredcites →https://doi.org/10.1186/1750-1326-5-33openalex-snapshot

Phosphorylation regulates proteasomal-mediated degradation and solubility of TAR DNA binding protein-43 C-terminal fragments

inferredcites →https://doi.org/10.1186/1750-1326-6-57openalex-snapshot

C-Jun N-terminal kinase controls TDP-43 accumulation in stress granules induced by oxidative stress

inferredcites →https://doi.org/10.1186/1750-1326-6-73openalex-snapshot

Expression of mutant TDP-43 induces neuronal dysfunction in transgenic mice

inferredcites →https://doi.org/10.1186/1750-1326-7-1openalex-snapshot

Adeno-associated virus-mediated brain delivery of 5-lipoxygenase modulates the AD-like phenotype of APP mice

inferredcites →https://doi.org/10.1186/1750-1326-7-54openalex-snapshot

Endogenous TDP-43, but not FUS, contributes to stress granule assembly via G3BP

inferredcites →https://doi.org/10.1186/s13024-018-0237-9openalex-snapshot

Pathological phosphorylation of tau and TDP-43 by TTBK1 and TTBK2 drives neurodegeneration

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A phase 2 double-blind placebo-controlled 24-week treatment clinical study of the p38 alpha kinase inhibitor neflamapimod in mild Alzheimer’s disease

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Genetics of familial amyotrophic lateral sclerosis

inferredcites →https://doi.org/10.1242/jcs.038950openalex-snapshot

Structural determinants of the cellular localization and shuttling of TDP-43

inferredcites →https://doi.org/10.1371/journal.pgen.1004803openalex-snapshot

The Tau Tubulin Kinases TTBK1/2 Promote Accumulation of Pathological TDP-43

inferredcites →https://doi.org/10.1371/journal.pone.0023075openalex-snapshot

Hyperphosphorylation as a Defense Mechanism to Reduce TDP-43 Aggregation

inferredcites →https://doi.org/10.1371/journal.pone.0090452openalex-snapshot

Casein Kinase II Induced Polymerization of Soluble TDP-43 into Filaments Is Inhibited by Heat Shock Proteins

inferredcites →https://doi.org/10.1523/jneurosci.2911-10.2010openalex-snapshot

Phosphorylation Promotes Neurotoxicity in aCaenorhabditis elegansModel of TDP-43 Proteinopathy

inferredcites →https://doi.org/10.1523/jneurosci.3389-17.2018openalex-snapshot

Arginine Methyltransferase PRMT8 Provides Cellular Stress Tolerance in Aging Motoneurons

inferredcites →https://doi.org/10.1523/jneurosci.4988-09.2010openalex-snapshot

Cytoplasmic Mislocalization of TDP-43 Is Toxic to Neurons and Enhanced by a Mutation Associated with Familial Amyotrophic Lateral Sclerosis

inferredcites →https://doi.org/10.15252/embj.201797452openalex-snapshot

A single N‐terminal phosphomimic disrupts TDP‐43 polymerization, phase separation, and RNA splicing

inferredcites →https://doi.org/10.15252/embj.2021108443openalex-snapshot

Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation

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p38 MAP Kinase Inhibitors as Potential Therapeutic Drugs for Neural Diseases

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Expression and Purification of Recombinant Skd3 (Human ClpB) Protein and Tobacco Etch Virus (TEV) Protease from Escherichia coli

inferredcites →https://doi.org/10.2741/2727openalex-snapshot

Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease

inferredcites →https://doi.org/10.3389/fnmol.2017.00046openalex-snapshot

Cytoplasmic Relocalization of TAR DNA-Binding Protein 43 Is Not Sufficient to Reproduce Cellular Pathologies Associated with ALS In vitro

inferredcites →https://doi.org/10.3389/fnmol.2019.00025openalex-snapshot

Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis

inferredcites →https://doi.org/10.3390/ijms21155485openalex-snapshot

P38α MAPK Signaling—A Robust Therapeutic Target for Rab5-Mediated Neurodegenerative Disease

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Atypical p38 Signaling, Activation, and Implications for Disease

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1002/bies.70084openalex-snapshot

TDP‐43 Phosphorylation: Pathological Modification or Protective Factor Antagonizing TDP‐43 Aggregation in Neurodegenerative Diseases?

inferred← citeshttps://doi.org/10.1021/acs.chemrev.2c00851openalex-snapshot

Regulation of Biomolecular Condensates by Poly(ADP-ribose)

inferred← citeshttps://doi.org/10.1038/s41586-023-06405-wopenalex-snapshot

TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP

inferred← citeshttps://doi.org/10.1038/s42003-025-07456-7openalex-snapshot

TDP-43 nuclear retention is antagonized by hypo-phosphorylation of its C-terminus in the cytoplasm

inferred← citeshttps://doi.org/10.1101/2022.08.14.503569openalex-snapshot

The post-translational modification SUMO affects TDP-43 phase separation, compartmentalization, and aggregation in a zebrafish model

inferred← citeshttps://doi.org/10.1101/2024.06.18.599616openalex-snapshot

The Interplay of Acetylation and Ubiquitination Controls PRMT1 Homeostasis

inferred← citeshttps://doi.org/10.1126/science.adv3301openalex-snapshot

Short RNA chaperones promote aggregation-resistant TDP-43 conformers to mitigate neurodegeneration

inferred← citeshttps://doi.org/10.1172/jci168549openalex-snapshot

Disrupting pathologic phase transitions in neurodegeneration

inferred← citeshttps://doi.org/10.1186/s13024-023-00698-1openalex-snapshot

Nuclear-import receptors as gatekeepers of pathological phase transitions in ALS/FTD

inferred← citeshttps://doi.org/10.1186/s40478-023-01592-zopenalex-snapshot

Targeting the glycine-rich domain of TDP-43 with antibodies prevents its aggregation in vitro and reduces neurofilament levels in vivo

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