ReviewCell motility and the cytoskeleton2009
Review of the mechanism of processive actin filament elongation by formins.
Review in Cell motility and the cytoskeleton, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 135 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
135 citing papers in PubMed.
- Human formin FHOD3-mediated actin elongation is required for sarcomere integrity in cardiomyocytes.eLife · 2025Article
- Cytoskeletal Proteins and Alzheimer's Disease Pathogenesis: Focusing on the Interplay with Tau Pathology.Biomolecules · 2025Review
- Mechanisms of force transmission on cytokinesis Formin Cdc12 in fission yeast revealed by coiled-coil force sensors.bioRxiv : the preprint server for biology · 2025Article
- Autism spectrum disorder related phenotypes in a mouse model lacking the neuronal actin binding protein profilin 2.Frontiers in cellular neuroscience · 2025Article
- The mode of subunit addition regulates the processive elongation of actin filaments by formin.The Journal of biological chemistry · 2025Article
- Prediction of the essential intermolecular contacts for side-binding of VASP on F-actin.Cytoskeleton (Hoboken, N.J.) · 2024Article
- Article
- Diaph1 knockout inhibits mouse primordial germ cell proliferation and affects gonadal development.Reproductive biology and endocrinology : RB&E · 2024Article
- Article
- CHLOROPLAST UNUSUAL POSITIONING 1 is a plant-specific actin polymerization factor regulating chloroplast movement.The Plant cell · 2024Article
- Origin and arrangement of actin filaments for gliding motility in apicomplexan parasites revealed by cryo-electron tomography.Nature communications · 2023Article
- The actin cytoskeleton: Morphological changes in pre- and fully developed lung cancer.Biophysics reviews · 2022Review
- Optineurin links Hace1-dependent Rac ubiquitylation to integrin-mediated mechanotransduction to control bacterial invasion and cell division.Nature communications · 2022Article
- Review
- How torque on formins is relaxed strongly affects cellular swirling.Biophysical journal · 2022Article
- The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022Review
- Molecular Dissection of DAAM Function during Axon Growth in Drosophila Embryonic Neurons.Cells · 2022Article
- Nucleation limits the lengths of actin filaments assembled by formin.Biophysical journal · 2021Article
- Formin Cdc12's specific actin assembly properties are tailored for cytokinesis in fission yeast.Biophysical journal · 2021Article
- The formin inhibitor SMIFH2 inhibits members of the myosin superfamily.Journal of cell science · 2021Article
75 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
We review recent structural and biophysical studies of the mechanism of action of formins, proteins that direct the assembly of unbranched actin filaments for cytokinetic contractile rings and other cellular structures. Formins use free actin monomers to nucleate filaments and then remain bound to the barbed ends of these filaments as they elongate. In addition to variable regulatory domains, formins typically have formin homology 1 (FH1) and formin homology 2 (FH2) domains. FH1 domains have multiple binding sites for profilin, an abundant actin monomer binding protein. FH2 homodimers encircle the barbed end of a filament. Most FH2 domains inhibit actin filament elongation, but FH1 domains concentrate multiple profilin-actin complexes near the end of the filament. FH1 domains transfer actin very rapidly onto the barbed end of the filament, allowing elongation at rates that exceed the rate of elongation by the addition of free actin monomers diffusing in solution. Binding of actin to the end of the filament provides the energy for the highly processive movement of the FH2 as a filament adds thousands of actin subunits. These biophysical insights provide the context to understand how formins contribute to actin assembly in cells. Cell Motil. Cytoskeleton 2009. (c) 2009 Wiley-Liss, Inc.
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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.