ArticleJournal of molecular biology2020
Profilin's Affinity for Formin Regulates the Availability of Filament Ends for Actin Monomer Binding.
Article in Journal of molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Article
- FGF-Mediated Axon Guidance: Role of Downstream Signaling Pathways in Cytoskeletal Control.Cells · 2025Review
- Genome-Wide Characterization and Analysis of theGenes · 2025Article
- The mode of subunit addition regulates the processive elongation of actin filaments by formin.The Journal of biological chemistry · 2025Article
- Article
- Single particle cryo-EM analysis of Rickettsia conorii Sca2 reveals a formin-like core.Journal of structural biology · 2023Article
- The Actin Regulators Involved in the Function and Related Diseases of Lymphocytes.Frontiers in immunology · 2022Review
- Nucleation limits the lengths of actin filaments assembled by formin.Biophysical journal · 2021Article
- Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Nucleation-promoting proteins tightly regulate actin polymerization in cells. Whereas many of these proteins bind actin monomers directly, formins use the actin-binding protein profilin to dynamically load actin monomers onto their flexible Formin Homology 1 (FH1) domains. Following binding, FH1 domains deliver profilin-actin complexes to filament ends. To investigate profilin's role as an adaptor protein in formin-mediated elongation, we engineered a chimeric formin that binds actin monomers directly via covalent attachment of profilin to its binding site in the formin. This formin mediates slow filament elongation owing to a high probability of profilin binding at filament ends. Varying the position at which profilin is tethered to the formin alters the elongation rate by modulating profilin occupancy at the filament end. By regulating the availability of the barbed end, we propose that profilin binding establishes a secondary point of control over the rate of filament elongation mediated by formins. Profilin's differential affinities for actin monomers, barbed ends and polyproline are thus tuned to adaptively bridge actin and formins and optimize the rate of actin polymerization.
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Registered trials
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