Evidence map›Paper›PMID 11901171›Full record

ArticleThe Journal of cell biology2002

Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics.

Shoichiro Ono, Kanako Ono

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 135 papers.

0numbers the graph read from it
0cells of the map it votes in
135citing papers in PubMed
8.5field-weighted citation impact, top 2% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

135 citing papers in PubMed, 255 citations in OpenAlex.

  1. Alterations of actin in aging.Journal of cell science · 2026
    Review
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  14. The sole essential low molecular weight tropomyosin isoform ofbioRxiv : the preprint server for biology · 2024
    Article
  15. Article
  16. Article
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75 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Shoichiro OnoDepartment of Pathology, Emory University, Atlanta, Georgia 30322, USA. sono@emory.edu
Kanako Ono
Emory University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tropomyosin binds to actin filaments and is implicated in stabilization of actin cytoskeleton. We examined biochemical and cell biological properties of Caenorhabditis elegans tropomyosin (CeTM) and obtained evidence that CeTM is antagonistic to ADF/cofilin-dependent actin filament dynamics. We purified CeTM, actin, and UNC-60B (a muscle-specific ADF/cofilin isoform), all of which are derived from C. elegans, and showed that CeTM and UNC-60B bound to F-actin in a mutually exclusive manner. CeTM inhibited UNC-60B-induced actin depolymerization and enhancement of actin polymerization. Within isolated native thin filaments, actin and CeTM were detected as major components, whereas UNC-60B was present at a trace amount. Purified UNC-60B was unable to interact with the native thin filaments unless CeTM and other associated proteins were removed by high-salt extraction. Purified CeTM was sufficient to restore the resistance of the salt-extracted filaments from UNC-60B. In muscle cells, CeTM and UNC-60B were localized in different patterns. Suppression of CeTM by RNA interference resulted in disorganized actin filaments and paralyzed worms in wild-type background. However, in an ADF/cofilin mutant background, suppression of CeTM did not worsen actin organization and worm motility. These results suggest that tropomyosin is a physiological inhibitor of ADF/cofilin-dependent actin dynamics.

Indexed as

Actin CytoskeletonActin Depolymerizing FactorsAnimalsBinding SitesCaenorhabditis elegansCaenorhabditis elegans ProteinsCell DifferentiationDestrinGene Expression Regulation, DevelopmentalGenetic VectorsHelminth ProteinsMicrofilament ProteinsMuscle Fibers, SkeletalMusclesMutationPolymersActin Depolymerizing FactorsCaenorhabditis elegans ProteinsDestrinHelminth ProteinsMicrofilament ProteinsPolymersProtein IsoformsRNATropomyosinUNC-60 protein, C elegans

Identifiers

PMID11901171
PMCPMC2173459
OpenAlexW2140686956

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

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.