ArticleThe Journal of biological chemistry2014
The role of formin tails in actin nucleation, processive elongation, and filament bundling.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Constitutively active mDia1 enables visualization of actin assembly in filopodia.bioRxiv : the preprint server for biology · 2026Article
- Regulation of the formin INF2 by actin monomers and calcium/calmodulin.The Journal of cell biology · 2026Article
- 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
- FHOD-1 and profilin protect sarcomeres against contraction-induced deformation> inMolecular biology of the cell · 2024Article
- Actin filament dynamics at barbed ends: New structures, new insights.Current opinion in cell biology · 2024Review
- FHOD-1/profilin-mediated actin assembly protects sarcomeres against contraction-induced deformation inbioRxiv : the preprint server for biology · 2024Article
- Nucleation limits the lengths of actin filaments assembled by formin.Biophysical journal · 2021Article
- Profilin and Mical combine to impair F-actin assembly and promote disassembly and remodeling.Nature communications · 2021Article
- DAAM2 Variants Cause Nephrotic Syndrome via Actin Dysregulation.American journal of human genetics · 2020Article
- Mechanochemical coupling of formin-induced actin interaction at the level of single molecular complex.Biomechanics and modeling in mechanobiology · 2020Article
- Defects in G-Actin Incorporation into Filaments in Myoblasts Derived from Dysferlinopathy Patients Are Restored by Dysferlin C2 Domains.International journal of molecular sciences · 2019Article
- Review
- Neuronal drebrin A directly interacts with mDia2 formin to inhibit actin assembly.Molecular biology of the cell · 2019Article
- Mechanisms of formin-mediated actin assembly and dynamics.Biophysical reviews · 2018Review
- Article
- The neuron-specific formin Delphilin nucleates nonmuscle actin but does not enhance elongation.Molecular biology of the cell · 2018Article
- Article
- The activities of the C-terminal regions of the formin protein disheveled-associated activator of morphogenesis (DAAM) in actin dynamics.The Journal of biological chemistry · 2017Article
- INF2- and FHOD-related formins promote ovulation in the somatic gonad of C. elegans.Cytoskeleton (Hoboken, N.J.) · 2016Article
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Authors and funding
3 authors.
Funding
Abstract
Formins are multidomain proteins that assemble actin in a wide variety of biological processes. They both nucleate and remain processively associated with growing filaments, in some cases accelerating filament growth. The well conserved formin homology 1 and 2 domains were originally thought to be solely responsible for these activities. Recently a role in nucleation was identified for the Diaphanous autoinhibitory domain (DAD), which is C-terminal to the formin homology 2 domain. The C-terminal tail of the Drosophila formin Cappuccino (Capu) is conserved among FMN formins but distinct from other formins. It does not have a DAD domain. Nevertheless, we find that Capu-tail plays a role in filament nucleation similar to that described for mDia1 and other formins. Building on this, replacement of Capu-tail with DADs from other formins tunes nucleation activity. Capu-tail has low-affinity interactions with both actin monomers and filaments. Removal of the tail reduces actin filament binding and bundling. Furthermore, when the tail is removed, we find that processivity is compromised. Despite decreased processivity, the elongation rate of filaments is unchanged. Again, replacement of Capu-tail with DADs from other formins tunes the processive association with the barbed end, indicating that this is a general role for formin tails. Our data show a role for the Capu-tail domain in assembling the actin cytoskeleton, largely mediated by electrostatic interactions. Because of its multifunctionality, the formin tail is a candidate for regulation by other proteins during cytoskeletal rearrangements.
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