ArticleThe EMBO journal2006
A CapG gain-of-function mutant reveals critical structural and functional determinants for actin filament severing.
Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 29 citations in OpenAlex.
- CAPG serves as a prognostic biomarker and promotes proliferation and migration in pancreatic ductal adenocarcinoma.PloS one · 2026Article
- Proteomic Analysis of Thin Filament Components Elucidates Changes in Spastic Muscle Sarcomere After Stroke.International journal of molecular sciences · 2025Article
- Repeated FRAP of the actin-binding protein CapG in the cell nucleus-a functional assay for EGF signaling in the single live breast cancer cell.Scientific reports · 2024Article
- Deciphering genetic and nongenetic factors underlying tumour dormancy: insights from multiomics analysis of two syngeneic MRD models of melanoma and leukemia.Biological research · 2024Article
- CAPG Is Required for Ebola Virus Infection by Controlling Virus Egress from Infected Cells.Viruses · 2022Article
- Structural Basis for pH-mediated Regulation of F-actin Severing by Gelsolin Domain 1.Scientific reports · 2017Article
- Calcium-controlled conformational choreography in the N-terminal half of adseverin.Nature communications · 2015Article
- Gelsolin-Like Domain 3 Plays Vital Roles in Regulating the Activities of the Lily Villin/Gelsolin/Fragmin Superfamily.PloS one · 2015Article
- A nanobody targeting the F-actin capping protein CapG restrains breast cancer metastasis.Breast cancer research : BCR · 2013Article
- Global shapes of F-actin depolymerization-competent minimal gelsolins: insight into the role of g2-g3 linker in pH/Ca2+ insensitivity of the first half.The Journal of biological chemistry · 2013Article
- The C-terminal tail domain of metavinculin, vinculin's splice variant, severs actin filaments.The Journal of cell biology · 2012Article
- Calcium-sensitive activity and conformation of Caenorhabditis elegans gelsolin-like protein 1 are altered by mutations in the first gelsolin-like domain.The Journal of biological chemistry · 2011Article
- Visual insight into how low pH alone can induce actin-severing ability in gelsolin under calcium-free conditions.The Journal of biological chemistry · 2011Article
- Article
- Dynamics of the CapG actin-binding protein in the cell nucleus studied by FRAP and FCS.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2008Article
- Villin severing activity enhances actin-based motility in vivo.Molecular biology of the cell · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 3 institutions in 1 country.
Funding
Abstract
CapG is the only member of the gelsolin family unable to sever actin filaments. Changing amino acids 84-91 (severing domain) and 124-137 (WH2-containing segment) simultaneously to the sequences of gelsolin results in a mutant, CapG-sev, capable of severing actin filaments. The gain of severing function does not alter actin filament capping, but is accompanied by a higher affinity for monomeric actin, and the capacity to bind and sequester two actin monomers. Analysis of CapG-sev crystal structure suggests a more loosely folded inactive conformation than gelsolin, with a shorter S1-S2 latch. Calcium binding to S1 opens this latch and S1 becomes separated from a closely interfaced S2-S3 complex by an extended arm consisting of amino acids 118-137. Modeling with F-actin predicts that the length of this WH2-containing arm is critical for severing function, and the addition of a single amino acid (alanine or histidine) eliminates CapG-sev severing activity, confirming this prediction. We conclude that efficient severing utilizes two actin monomer-binding sites, and that the length of the WH2-containing segment is a critical functional determinant for severing.
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.