Composite
68%
Novelty
75%
Feasibility
60%
Impact
83%
Mechanistic
86%
Druggability
Safety
Confidence
48%

Mechanistic description

Symmetric dimethylation of arginine residues in the FUS RGG1/RGG2 domains by PRMT5/PRMT1 maintains FUS in a dynamic liquid phase-separated state by reducing inter-molecular beta-sheet propensity. ALS-linked mutations near the RGG domains reduce arginine methylation efficiency, shifting FUS toward an aggregation-prone unmethylated state. PRMT5 activator treatment in FUS-ALS iPSC motor neurons should restore arginine methylation stoichiometry and increase the concentration required for pathological aggregation by >3-fold.

Mechanism / pathway

  1. FUS
  2. Arginine methylation / RBP phase separation
  3. ALS

Evidence for (5)

  • ALS-FUS mutations cause abnormal PARylation and histone H1.2 interaction, leading to pathological changes.

    PMID:39167487 2024 Cell Rep
  • ALS-associated FUS mutation reshapes the RNA and protein composition of stress granules.

    PMID:39494508 2024 Nucleic Acids Res
  • A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation.

    PMID:26317470 2015 Cell
  • M6A-dependent RNA condensation underlies FUS autoregulation and can be harnessed for ALS therapy development.

    PMID:40700505 2025 Sci Adv
  • Pathogenesis of FUS-associated ALS and FTD: insights from rodent models.

    PMID:27600654 2016 Acta Neuropathol Commun

Evidence against (2)

Evidence matrix

5 supporting 0 contradicting
100% supporting

Supporting

  • ALS-FUS mutations cause abnormal PARylation and histone H1.2 interaction, leading to pathological changes. PMID:39167487 · 2024 · Cell Rep
  • ALS-associated FUS mutation reshapes the RNA and protein composition of stress granules. PMID:39494508 · 2024 · Nucleic Acids Res
  • A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation. PMID:26317470 · 2015 · Cell
  • M6A-dependent RNA condensation underlies FUS autoregulation and can be harnessed for ALS therapy development. PMID:40700505 · 2025 · Sci Adv
  • Pathogenesis of FUS-associated ALS and FTD: insights from rodent models. PMID:27600654 · 2016 · Acta Neuropathol Commun

Contradicting

No contradicting evidence recorded.

Cite this hypothesis

Cite this hypothesis
Citation

etl-backfill (2026). Arginine Methylation Loss on FUS RGG Domains Drives Irreversible Phase Transiti…. SciDEX hypothesis. https://prism.scidex.ai/hypotheses/897f3e4a-f96a-4a65-b3c8-61e20a1054da

BibTeX
@misc{scidex_hypothesis_897f3e4a,
  title        = {Arginine Methylation Loss on FUS RGG Domains Drives Irreversible Phase Transiti…},
  author       = {etl-backfill},
  year         = {2026},
  howpublished = {SciDEX hypothesis},
  url          = {https://prism.scidex.ai/hypotheses/897f3e4a-f96a-4a65-b3c8-61e20a1054da},
  note         = {SciDEX artifact hypothesis:897f3e4a-f96a-4a65-b3c8-61e20a1054da}
}

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POST /api/scidex/rpc
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