ArticleScience advances2024
Molecular mechanisms linking missense ACTG2 mutations to visceral myopathy.
Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Unmasking the "Braided" Bowel: Chronic Intestinal Pseudo-Obstruction-A Case Report.Diagnostics (Basel, Switzerland) · 2026Article
- Non-muscle tropomyosins inhibit myosin-19 and dynamically localize to mitochondrially associated actin filaments.The Journal of biological chemistry · 2026Article
- International Forum on Visceral Myopathy 2024: Advances in the Knowledge of the Disease.Neurogastroenterology and motility · 2026Review
- Clinical, manometric, genetic, and histologic associations in pediatric intestinal pseudo-obstruction: A case series.Journal of pediatric gastroenterology and nutrition · 2026Article
- R5 and R7 positions on fluoroquinolone scaffolds drive F-actin filament disruption.Scientific reports · 2026Article
- Dynamical features of smooth muscle actin pathological mutants: The arginine-257(258)-Cysteine cases.Computational and structural biotechnology journal · 2025Article
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Authors and funding
8 authors.
Funding
Abstract
Visceral myopathy is a life-threatening disease characterized by muscle weakness in the bowel, bladder, and uterus. Mutations in smooth muscle γ-actin (ACTG2) are the most common cause of the disease, but the mechanisms by which the mutations alter muscle function are unknown. Here, we examined four prevalent ACTG2 mutations (R40C, R148C, R178C, and R257C) that cause different disease severity and are spread throughout the actin fold. R178C displayed premature degradation, R148C disrupted interactions with actin-binding proteins, R40C inhibited polymerization, and R257C destabilized filaments. Because these mutations are heterozygous, we also analyzed 50/50 mixtures with wild-type (WT) ACTG2. The WT/R40C mixture impaired filament nucleation by leiomodin 1, and WT/R257C produced filaments that were easily fragmented by smooth muscle myosin. Smooth muscle tropomyosin isoform Tpm1.4 partially rescued the defects of R40C and R257C. Cryo-electron microscopy structures of filaments formed by R40C and R257C revealed disrupted intersubunit contacts. The biochemical and structural properties of the mutants correlate with their genotype-specific disease severity.
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