ArticleStructure (London, England : 1993)2015
Electrostatic interactions between the Bni1p Formin FH2 domain and actin influence actin filament nucleation.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 32 citations in OpenAlex.
- Human formin FHOD3-mediated actin elongation is required for sarcomere integrity in cardiomyocytes.eLife · 2025Article
- The mode of subunit addition regulates the processive elongation of actin filaments by formin.The Journal of biological chemistry · 2025Article
- Electrical Forces Regulate Single-Cell Wound Healing.Reviews of physiology, biochemistry and pharmacology · 2025Review
- Prediction of the essential intermolecular contacts for side-binding of VASP on F-actin.Cytoskeleton (Hoboken, N.J.) · 2024Article
- Parallel actin monomers in the 8S complex of actin-INF2.Journal of biomolecular structure & dynamics · 2023Article
- Evolutionary tuning of barbed end competition allows simultaneous construction of architecturally distinct actin structures.The Journal of cell biology · 2023Article
- Biochemical and mechanical regulation of actin dynamics.Nature reviews. Molecular cell biology · 2022Review
- A structural model of the profilin-formin pacemaker system for actin filament elongation.Scientific reports · 2022Article
- Towards a structural understanding of the remodeling of the actin cytoskeleton.Seminars in cell & developmental biology · 2020Review
- Multiscale simulation of actin filaments and actin-associated proteins.Biophysical reviews · 2018Review
- Mechanisms of formin-mediated actin assembly and dynamics.Biophysical reviews · 2018Review
- Article
- Computational modeling highlights the role of the disordered Formin Homology 1 domain in profilin-actin transfer.FEBS letters · 2018Article
- Article
- The neuron-specific formin Delphilin nucleates nonmuscle actin but does not enhance elongation.Molecular biology of the cell · 2018Article
- Actin and Actin-Binding Proteins.Cold Spring Harbor perspectives in biology · 2016Review
- Role of the C-terminal Extension of Formin 2 in Its Activation by Spire Protein and Processive Assembly of Actin Filaments.The Journal of biological chemistry · 2016Article
- Formin and capping protein together embrace the actin filament in a ménage à trois.Nature communications · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Formins catalyze nucleation and growth of actin filaments. Here, we study the structure and interactions of actin with the FH2 domain of budding yeast formin Bni1p. We built an all-atom model of the formin dimer on an Oda actin filament 7-mer and studied structural relaxation and interprotein interactions by molecular dynamics simulations. These simulations produced a refined model for the FH2 dimer associated with the barbed end of the filament and showed electrostatic interactions between the formin knob and actin target-binding cleft. Mutations of two formin residues contributing to these interactions (R1423N, K1467L, or both) reduced the interaction energies between the proteins, and in coarse-grained simulations, the formin lost more interprotein contacts with an actin dimer than with an actin 7-mer. Biochemical experiments confirmed a strong influence of these mutations on Bni1p-mediated actin filament nucleation, but not elongation, suggesting that different interactions contribute to these two functions of formins.
Indexed as
Identifiers
What OpenQuestion holds
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.