ArticleEuropean journal of cell biology2022
Biochemical characterization of actin assembly mechanisms with ALS-associated profilin variants.
Article in European journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 21 citations in OpenAlex.
- Alterations of actin in aging.Journal of cell science · 2026Review
- Constitutively active mDia1 enables visualization of actin assembly in filopodia.bioRxiv : the preprint server for biology · 2026Article
- Profilin and Non-Canonical Wnt Signaling: Coordinating Cytoskeletal Dynamics from Development to Disease.Journal of developmental biology · 2025Review
- Using ALS to understand profilin 1's diverse roles in cellular physiology.Cytoskeleton (Hoboken, N.J.) · 2025Review
- Label-free proteomic analysis of Duchenne and Becker muscular dystrophy showed decreased sarcomere proteins and increased ubiquitination-related proteins.Scientific reports · 2025Article
- Coordination of actin plus-end dynamics by IQGAP1, formin, and capping protein.The Journal of cell biology · 2024Article
- Prolonged depletion of profilin 1 or F-actin causes an adaptive response in microtubules.The Journal of cell biology · 2024Article
- Coordination of actin plus-end dynamics by IQGAP1, formin, and capping protein.bioRxiv : the preprint server for biology · 2024Article
- Expression of ALS-PFN1 impairs vesicular degradation in iPSC-derived microglia.Nature communications · 2024Article
- Cyclase-associated protein interacts with actin filament barbed ends to promote depolymerization and formin displacement.The Journal of biological chemistry · 2023Article
- The formin DAAM1 regulates the deubiquitinase activity of USP10 and integrin homeostasis.European journal of cell biology · 2023Article
- Nuclear pore complex and nucleocytoplasmic transport disruption in neurodegeneration.FEBS letters · 2023Review
- Cytoskeletal adaptation following long-term dysregulation of actomyosin in neuronal processes.bioRxiv : the preprint server for biology · 2023Article
- Purification of human β- and γ-actin from budding yeast.Journal of cell science · 2023Article
- Current insights in the molecular genetic pathogenesis of amyotrophic lateral sclerosis.Frontiers in neuroscience · 2023Review
- Multiple roles for the cytoskeleton in ALS.Experimental neurology · 2022Review
- Visualizing Actin and Microtubule Coupling Dynamics In Vitro by Total Internal Reflection Fluorescence (TIRF) Microscopy.Journal of visualized experiments : JoVE · 2022Article
- Visualizing molecules of functionaleLife · 2022Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Eight separate mutations in the actin-binding protein profilin-1 have been identified as a rare cause of amyotrophic lateral sclerosis (ALS). Profilin is essential for many neuronal cell processes through its regulation of lipids, nuclear signals, and cytoskeletal dynamics, including actin filament assembly. Direct interactions between profilin and actin monomers inhibit actin filament polymerization. In contrast, profilin can also stimulate polymerization by simultaneously binding actin monomers and proline-rich tracts found in other proteins. Whether the ALS-associated mutations in profilin compromise these actin assembly functions is unclear. We performed a quantitative biochemical comparison of the direct and formin mediated impact for the eight ALS-associated profilin variants on actin assembly using classic protein-binding and single-filament microscopy assays. We determined that the binding constant of each profilin for actin monomers generally correlates with the actin nucleation strength associated with each ALS-related profilin. In the presence of formin, the A20T, R136W, Q139L, and C71G variants failed to activate the elongation phase of actin assembly. This diverse range of formin-activities is not fully explained through profilin-poly-L-proline (PLP) interactions, as all ALS-associated variants bind a formin-derived PLP peptide with similar affinities. However, chemical denaturation experiments suggest that the folding stability of these profilins impact some of these effects on actin assembly. Thus, changes in profilin protein stability and alterations in actin filament polymerization may both contribute to the profilin-mediated actin disruptions in ALS.
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