ArticleBMC neuroscience2015
Profilin 1 with the amyotrophic lateral sclerosis associated mutation T109M displays unaltered actin binding and does not affect the actin cytoskeleton.
Article in BMC neuroscience, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.
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Who cites it
18 citing papers in PubMed, 1 synthesis or guideline pooled it, 24 citations in OpenAlex.
- A Systematic and Comprehensive Review on Disease-Causing Genes in Amyotrophic Lateral Sclerosis.Journal of molecular neuroscience : MN · 2020Pooled it
- 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
- Article
- The Amyotrophic Lateral Sclerosis M114T PFN1 Mutation Deregulates Alternative Autophagy Pathways and Mitochondrial Homeostasis.International journal of molecular sciences · 2022Article
- Biochemical characterization of actin assembly mechanisms with ALS-associated profilin variants.European journal of cell biology · 2022Article
- Profilin Isoforms in Health and Disease - All the Same but Different.Frontiers in cell and developmental biology · 2021Review
- The Peripheral Nervous System in Amyotrophic Lateral Sclerosis: Opportunities for Translational Research.Frontiers in neuroscience · 2019Review
- Activation of Cofilin Increases Intestinal PermeabilityFrontiers in physiology · 2019Article
- Changes in biophysical characteristics of PFN1 due to mutation causing amyotrophic lateral sclerosis.Metabolic brain disease · 2018Article
- Dysregulation of a novel miR-1825/TBCB/TUBA4A pathway in sporadic and familial ALS.Cellular and molecular life sciences : CMLS · 2018Article
- Stability of an aggregation-prone partially folded state of human profilin-1 correlates with aggregation propensity.The Journal of biological chemistry · 2018Article
- Cucurbitacin E Inhibits Proliferation and Migration of Intestinal Epithelial Cells via Activating Cofilin.Frontiers in physiology · 2018Article
- Profilin Directly Promotes Microtubule Growth through Residues Mutated in Amyotrophic Lateral Sclerosis.Current biology : CB · 2017Article
- Profilin1 biology and its mutation, actin(g) in disease.Cellular and molecular life sciences : CMLS · 2017Review
- Mutant Profilin1 transgenic mice recapitulate cardinal features of motor neuron disease.Human molecular genetics · 2017Article
- BDNF/trkB Induction of Calcium Transients through CaFrontiers in molecular neuroscience · 2017Article
- Mutant Profilin1 Aggregation in Amyotrophic Lateral Sclerosis: An in Vivo Biochemical Analysis.Basic and clinical neuroscienceArticle
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe recent identification of several mutations in PFN1, a protein involved in actin dynamics, strengthens the hypothesis that pathology of amyotrophic lateral sclerosis is linked to cytoskeletal defects. Impaired actin binding is a common denominator of several PFN1 mutations associated with amyotrophic lateral sclerosis, although further mechanisms may also contribute to the death of motor neurons. In this study we examine the actin binding properties of PFN1 carrying the causal T109M mutation and its effects on the actin cytoskeleton.
methodsActin binding of PFN1 T109M was examined by co-immunoprecipitation experiments, a split luciferase complementation assay and a pulldown assay with recombinant PFN1. The actin cytoskeleton was investigated by fluorescence microscopy and by ultracentrifuge separation of globular and filamentous actin fractions followed by Western blotting.
resultsUsing different technical approaches we show that PFN1 T109M displays unaltered actin binding. Furthermore we show that the actin cytoskeleton is not affected by PFN1 carrying the T109M mutation.
conclusionOur data suggest that actin independent mechanisms contribute to the pathogenicity of PFN1 T109M and possibly other PFN1 mutations.
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