ArticleMolecular biology of the cell2012
Autoinhibition of the formin Cappuccino in the absence of canonical autoinhibitory domains.
Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed.
- Impact of N-terminal dimerization on formin homology 1 domain polymer dynamics and actin assembly.Biophysical journal · 2026Article
- The Cappuccino interactome reveals an intracellular role for Semaphorin-2a inbioRxiv : the preprint server for biology · 2026Article
- Regulation of the formin INF2 by actin monomers and calcium/calmodulin.The Journal of cell biology · 2026Article
- Impact of N-terminal dimerization on formin homology 1 domain polymer dynamics and actin assembly.bioRxiv : the preprint server for biology · 2025Article
- Human formin FHOD3-mediated actin elongation is required for sarcomere integrity in cardiomyocytes.eLife · 2025Article
- Alterations to the broad-spectrum formin inhibitor SMIFH2 modulate potency but not specificity.Scientific reports · 2022Article
- Spire stimulates nucleation by Cappuccino and binds both ends of actin filaments.Molecular biology of the cell · 2020Article
- Formin 2 Regulates Lysosomal Degradation of Wnt-Associated β-Catenin in Neural Progenitors.Cerebral cortex (New York, N.Y. : 1991) · 2019Article
- The neuron-specific formin Delphilin nucleates nonmuscle actin but does not enhance elongation.Molecular biology of the cell · 2018Article
- Article
- Roles of actin binding proteins in mammalian oocyte maturation and beyond.Cell cycle (Georgetown, Tex.) · 2016Review
- Article
- Metavinculin Tunes the Flexibility and the Architecture of Vinculin-Induced Bundles of Actin Filaments.Journal of molecular biology · 2015Article
- Article
- Drosophila Cappuccino alleles provide insight into formin mechanism and role in oogenesis.Molecular biology of the cell · 2015Article
- Drosophila comes of age as a model system for understanding the function of cytoskeletal proteins in cells, tissues, and organisms.Cytoskeleton (Hoboken, N.J.) · 2015Review
- Filament assembly by Spire: key residues and concerted actin binding.Journal of molecular biology · 2015Article
- Regulation of the formin Cappuccino is critical for polarity of Drosophila oocytes.Cytoskeleton (Hoboken, N.J.) · 2015Article
- The role of formin tails in actin nucleation, processive elongation, and filament bundling.The Journal of biological chemistry · 2014Article
- Interaction between microtubules and the Drosophila formin Cappuccino and its effect on actin assembly.The Journal of biological chemistry · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Formins are a conserved family of proteins known to enhance actin polymerization. Most formins are regulated by an intramolecular interaction. The Drosophila formin, Cappuccino (Capu), was believed to be an exception. Capu does not contain conserved autoinhibitory domains and can be regulated by a second protein, Spire. We report here that Capu is, in fact, autoinhibited. The N-terminal half of Capu (Capu-NT) potently inhibits nucleation and binding to the barbed end of elongating filaments by the C-terminal half of Capu (Capu-CT). Hydrodynamic analysis indicates that Capu-NT is a dimer, similar to the N-termini of other formins. These data, combined with those from circular dichroism, suggest, however, that it is structurally distinct from previously described formin inhibitory domains. Finally, we find that Capu-NT binds to a site within Capu-CT that overlaps with the Spire-binding site, the Capu-tail. We propose models for the interaction between Spire and Capu in light of the fact that Capu can be regulated by autoinhibition.
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.