ID: 897f3e4a-f96a-4a65-b3c8-61e20a1054da
Hypothesis

Arginine Methylation Loss on FUS RGG Domains Drives Irreversible Phase Transition to Amyloid in ALS

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.
🧬 FUS🩺 als🎯 Composite 68%💱 $0.58▲10.7%open
neurodegeneration
EvidencePending (0%)📖 5 cit🗣 1 debates 5 support 2 oppose
✓ All Quality Gates Passed
Mechanistic 0.86 (15%) Evidence 0.48 (15%) Novelty 0.75 (12%) Feasibility 0.60 (12%) Impact 0.83 (12%) Druggability 0.00 (10%) Safety 0.00 (8%) Competition 0.00 (6%) Data Avail. 0.00 (5%) Reproducible 0.00 (5%) KG Connect 0.37 (8%) 0.680 composite

🧪 Overview

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

🧬 Curated Mechanism Pathway

Curated pathway from expert analysis

flowchart TD
    A["FUS RGG1 RGG2 Domains<br/>RNA-Binding Protein in Motor Neurons"]
    B["PRMT1 and PRMT5 Activity<br/>Symmetric Dimethylarginine on RGG Repeats"]
    C["Dynamic Liquid Phase Separation<br/>Inter-molecular Beta-Sheet Propensity Reduced"]
    D["ALS-Linked FUS Mutations<br/>Near RGG Domains"]
    E["Reduced Arginine Methylation Efficiency<br/>Unmethylated FUS Accumulates"]
    F["Increased Beta-Sheet Propensity<br/>Aggregation-Prone Confirmation"]
    G["Insoluble FUS Amyloid Aggregates<br/>ALS FTD Pathology"]
    H["PRMT5 Activator Treatment<br/>Restores Methylation Stoichiometry"]
    A --> B
    B --> C
    D --> E
    E --> F
    F --> G
    H -.->|"3-fold aggregation threshold increase"| B
    style D fill:#7b1fa2,stroke:#ce93d8,color:#ce93d8
    style G fill:#b71c1c,stroke:#ef9a9a,color:#ef9a9a
    style H fill:#1b5e20,stroke:#a5d6a7,color:#a5d6a7

⚖️ Evidence

⚖️ Evidence Matrix5 supports0 contradicts
Supports
ALS-FUS mutations cause abnormal PARylation and histone H1.2 interaction, leading to pathological changes.
Cell Rep2024PMID:39167487medium
Supports
ALS-associated FUS mutation reshapes the RNA and protein composition of stress granules.
Nucleic Acids Res2024PMID:39494508medium
Supports
A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation.
Cell2015PMID:26317470medium
Supports
M6A-dependent RNA condensation underlies FUS autoregulation and can be harnessed for ALS therapy development.
Sci Adv2025PMID:40700505medium
Supports
Pathogenesis of FUS-associated ALS and FTD: insights from rodent models.
Acta Neuropathol Commun2016PMID:27600654medium
📖 Linked Papers

No linked papers recorded for this hypothesis yet.

🏥 Translation

🧬 3D Protein Structure — FUS

🧬 PDB 4FDD Click to expand

Experimental structure from RCSB PDB | Powered by Mol*

💉 Clinical Trials

No clinical trials data linked to this hypothesis yet.

No curated ClinVar variants loaded for this hypothesis.

Run scripts/backfill_clinvar_variants.py to fetch P/LP/VUS variants.

🔍 Search ClinVar for FUS →

No DepMap CRISPR Chronos data found for FUS.

Run python3 scripts/backfill_hypothesis_depmap.py to populate.

🏆 Tournament

🏆 Arenas / Elo

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📊 Market Indicators

7d Trend
Stable
7d Momentum
▼ 0.3%
Volatility
Medium
0.0282
Events (7d)
2
Price History
▲10.7%

💾 Resource Usage

No resource usage or linked notebooks recorded for this hypothesis yet.

Metadatasource: v1_phase_c_backfill · origin_type: literature_mining
sourcev1_phase_c_backfill
origin_typeliterature_mining
_schema_version1
📊 Evidence Profile
Evidence Balance
+0%
Certainty
0%
Debates
0
Incoming
0
Outgoing
0
0 supporting 0 contradicting 0 neutral
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