ArticleNature communications2015
The structure of FMNL2-Cdc42 yields insights into the mechanism of lamellipodia and filopodia formation.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 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
52 citing papers in PubMed, 82 citations in OpenAlex.
- Structural basis for membrane-dependent positive feedback regulation of DOCK11 by activated Cdc42.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Daam-, FMNL-, and mDia-family formins jointly regulate cortical actin dynamics in melanoma cells.Cell communication and signaling : CCS · 2026Article
- Cdc42 and Rac2 act through the formin-like Frl/FMNL to control lamellocyte shape and encapsulation of parasitoid wasp eggs in Drosophila.PLoS pathogens · 2026Article
- Regulation of the formin INF2 by actin monomers and calcium/calmodulin.The Journal of cell biology · 2026Article
- Spatially distinct FRL and Ena dependent actin networks coordinate nuclear positioning in Drosophila nurse cells.PLoS genetics · 2026Article
- Inhibition of CDC42 in adenomyosis reduces the proliferation of endometrial stromal cells and the migration of epithelial cells.American journal of translational research · 2026Article
- Modulation of host functions by bacterial serine/threonine protein kinase effector proteins.The Journal of biological chemistry · 2025Review
- Live-cell magnetic manipulation of recycling endosomes reveals their direct effect on actin protrusions to promote invasive migration.Science advances · 2025Article
- The formin FMNL2 plays a role in the response of melanoma cells to substrate stiffness.BMC molecular and cell biology · 2025Article
- Insulin receptor tyrosine kinase substrate in health and disease (Review).Molecular medicine reports · 2025Review
- Electrical Forces Regulate Single-Cell Wound Healing.Reviews of physiology, biochemistry and pharmacology · 2025Review
- Disulfidptosis: a novel cell death modality induced by actin cytoskeleton collapse and a promising target for cancer therapeutics.Cell communication and signaling : CCS · 2024Review
- The Chlamydia pneumoniae effector SemD exploits its host's endocytic machinery by structural and functional mimicry.Nature communications · 2024Article
- Mitochondrially-associated actin waves maintain organelle homeostasis and equitable inheritance.Current opinion in cell biology · 2024Review
- Identification of an FMNL2 Interactome by Quantitative Mass Spectrometry.International journal of molecular sciences · 2024Article
- Cytoskeleton remodeling induced by SMYD2 methyltransferase drives breast cancer metastasis.Cell discovery · 2024Article
- FMNL1 and mDia1 promote efficient T cell migration through complex environments via distinct mechanisms.Frontiers in immunology · 2024Article
- Competition and Synergy of Arp2/3 and Formins in Nucleating Actin Waves.bioRxiv : the preprint server for biology · 2023Article
- Spatiotemporal Regulation of FMNL2 by N-Terminal Myristoylation and C-Terminal Phosphorylation Drives Rapid Filopodia Formation.Biomolecules · 2023Article
- FHODs: Nuclear tethered formins for nuclear mechanotransduction.Frontiers in cell and developmental biology · 2023Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Formins are actin polymerization factors that elongate unbranched actin filaments at the barbed end. Rho family GTPases activate Diaphanous-related formins through the relief of an autoregulatory interaction. The crystal structures of the N-terminal domains of human FMNL1 and FMNL2 in complex with active Cdc42 show that Cdc42 mediates contacts with all five armadillo repeats of the formin with specific interactions formed by the Rho-GTPase insert helix. Mutation of three residues within Rac1 results in a gain-of-function mutation for FMNL2 binding and reconstitution of the Cdc42 phenotype in vivo. Dimerization of FMNL1 through a parallel coiled coil segment leads to formation of an umbrella-shaped structure that—together with Cdc42—spans more than 15 nm in diameter. The two interacting FMNL-Cdc42 heterodimers expose six membrane interaction motifs on a convex protein surface, the assembly of which may facilitate actin filament elongation at the leading edge of lamellipodia and filopodia.
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.