ArticleCurrent biology : CB2014
INF2-mediated severing through actin filament encirclement and disruption.
Article in Current biology : CB, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 60 citations in OpenAlex.
- Phosphorylation-dependent interaction between VAP proteins and INF2 influences ER morphology.Current biology : CB · 2026Article
- Regulation of CFTR stability at the plasma membrane-Mechanisms and therapeutic opportunities in cystic fibrosis.FEBS letters · 2026Review
- Regulation of the formin INF2 by actin monomers and calcium/calmodulin.The Journal of cell biology · 2026Article
- Structural and functional dissection of the WH2/DAD motif of INF2, a formin linked to human inherited degenerative disorders.The FEBS journal · 2026Article
- Functional Differences Between Neuronal and Non-neuronal Isoforms of Drebrin.Journal of molecular biology · 2025Article
- Formin 3 stabilizes the cytoskeleton of Drosophila tendon cells, thus enabling them to resist muscle tensile forces.Journal of cell science · 2025Article
- Regulation of formin INF2 and its alteration in INF2-linked inherited disorders.Cellular and molecular life sciences : CMLS · 2024Review
- Article
- Disulfidptosis-associated lncRNAs predict breast cancer subtypes.Scientific reports · 2023Article
- Characterization of cytoskeletal and structural effects of INF2 variants causing glomerulopathy and neuropathy.Scientific reports · 2023Article
- Parallel actin monomers in the 8S complex of actin-INF2.Journal of biomolecular structure & dynamics · 2023Article
- Actin Bundles Dynamics and Architecture.Biomolecules · 2023Review
- Direct observation of the conformational states of formin mDia1 at actin filament barbed ends and along the filament.Molecular biology of the cell · 2023Article
- Bring the pain: wounding reveals a transition from cortical excitability to epithelial excitability inFrontiers in cell and developmental biology · 2023Review
- Whole exome/genome sequencing in cyclic vomiting syndrome reveals multiple candidate genes, suggesting a model of elevated intracellular cations and mitochondrial dysfunction.Frontiers in neurology · 2023Article
- MICAL-mediated oxidation of actin and its effects on cytoskeletal and cellular dynamics.Frontiers in cell and developmental biology · 2023Review
- Actin-Binding Proteins in Cardiac Hypertrophy.Cells · 2022Review
- Mff oligomerization is required for Drp1 activation and synergy with actin filaments during mitochondrial division.Molecular biology of the cell · 2021Article
- Dysregulated Dynein-Mediated Trafficking of Nephrin Causes INF2-related Podocytopathy.Journal of the American Society of Nephrology : JASN · 2021Article
- Self-DNA Sensing by cGAS-STING and TLR9 in Autoimmunity: Is the Cytoskeleton in Control?Frontiers in immunology · 2021Review
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
Abstract
backgroundINF2 is a formin protein with the unique ability to accelerate both actin polymerization and depolymerization, the latter requiring filament severing. Mutations in INF2 lead to the kidney disease focal segmental glomerulosclerosis (FSGS) and the neurological disorder Charcot-Marie Tooth disease (CMTD).
resultsHere, we compare the severing mechanism of INF2 with that of the well-studied severing protein cofilin. INF2, like cofilin, binds stoichiometrically to filament sides and severs in a manner that requires phosphate release from the filament. In contrast to cofilin, however, INF2 binds ADP and ADP-Pi filaments equally well. Furthermore, two-color total internal reflection fluorescence (TIRF) microscopy reveals that a low number of INF2 molecules, as few as a single INF2 dimer, are capable of severing, while measurable cofilin-mediated severing requires more extensive binding. Hence, INF2 is a more potent severing protein than cofilin. While a construct containing the FH1 and FH2 domains alone has some severing activity, addition of the C-terminal region increases severing potency by 40-fold, and we show that the WH2-resembling DAD motif is responsible for this increase. Helical 3D reconstruction from electron micrographs at 20 Å resolution provides a structure of filament-bound INF2, showing that the FH2 domain encircles the filament.
conclusionsWe propose a severing model in which FH2 binding and phosphate release causes local filament deformation, allowing the DAD to bind adjacent actin protomers, further disrupting filament structure.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.