ArticlePloS one2011
Structural and functional evaluation of C. elegans filamins FLN-1 and FLN-2.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- fln-2 isoform-specifically regulates Caenorhabditis elegans health span by affecting pharyngeal function.Scientific reports · 2026Article
- Article
- FLN-2 functions in parallel to LINC complexes and Cdc42/actin pathways during P-cell nuclear migration through constricted spaces inbioRxiv : the preprint server for biology · 2023Article
- Intracellular CaiScience · 2022Article
- FLN-1/filamin is required to anchor the actomyosin cytoskeleton and for global organization of sub-cellular organelles in a contractile tissue.Cytoskeleton (Hoboken, N.J.) · 2020Article
- Redox signaling modulates Rho activity and tissue contractility in theMolecular biology of the cell · 2020Article
- Kettin, the large actin-binding protein with multiple immunoglobulin domains, is essential for sarcomeric actin assembly and larval development in Caenorhabditis elegans.The FEBS journal · 2020Article
- A fln-2 mutation affects lethal pathology and lifespan in C. elegans.Nature communications · 2019Article
- Regulation of Actin Dynamics in theJournal of developmental biology · 2019Review
- Article
- Filamin and phospholipase C-ε are required for calcium signaling in the Caenorhabditis elegans spermatheca.PLoS genetics · 2013Article
- Filamins in mechanosensing and signaling.Annual review of biophysics · 2012Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Filamins are long, flexible, multi-domain proteins composed of an N-terminal actin-binding domain (ABD) followed by multiple immunoglobulin-like repeats (IgFLN). They function to organize and maintain the actin cytoskeleton, to provide scaffolds for signaling components, and to act as mechanical force sensors. In this study, we used transcript sequencing and homology modeling to characterize the gene and protein structures of the C. elegans filamin orthologs fln-1 and fln-2. Our results reveal that C. elegans FLN-1 is well conserved at the sequence level to vertebrate filamins, particularly in the ABD and several key IgFLN repeats. Both FLN-1 and the more divergent FLN-2 colocalize with actin in vivo. FLN-2 is poorly conserved, with at least 23 IgFLN repeats interrupted by large regions that appear to be nematode-specific. Our results indicate that many of the key features of vertebrate filamins are preserved in C. elegans FLN-1 and FLN-2, and suggest the nematode may be a very useful model system for further study of filamin function.
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Registered trials
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