Evidence map›Paper›PMID 25373779›Full record

ArticleDevelopmental cell2014

Cofilin-2 controls actin filament length in muscle sarcomeres.

Elena Kremneva, Maarit H Makkonen, Aneta Skwarek-Maruszewska, Gergana Gateva, Alphee Michelot, Roberto Dominguez, Pekka Lappalainen

Open access · bronzeAbstract read
In one paragraph

Article in Developmental cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

54 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
  2. Disease-associated mutations inbioRxiv : the preprint server for biology · 2026
    Article
  3. Amyloid Beta Oligomers as Early Triggers of Neuronal Cytoskeleton Dysfunction in Alzheimer's Disease.Pathophysiology : the official journal of the International Society for Pathophysiology · 2026
    Review
  4. Article
  5. Article
  6. Review
  7. Cofilin(s) and Mitochondria: Function Beyond Actin Dynamics.International journal of molecular sciences · 2025
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023
    Review
  16. Troponin and a Myopathy-Linked Mutation inInternational journal of molecular sciences · 2023
    Article
  17. Article
  18. Review
  19. Article
  20. The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 3 countries.

Elena KremnevaInstitute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland.
Maarit H MakkonenInstitute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland.
Aneta Skwarek-MaruszewskaInstitute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland.
Gergana GatevaInstitute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland.
Alphee MichelotLaboratoire de Physiologie Cellulaire et Végétale, Institut de Recherches en Technologies et Sciences pour le Vivant, iRTSV, CNRS/CEA/INRA/UJF, 38054 Grenoble, France.
Roberto DominguezDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
Pekka LappalainenInstitute of Biotechnology, University of Helsinki, P.O. Box 56, 00014 Helsinki, Finland. Electronic address: pekka.lappalainen@helsinki.fi.
University of Helsinki · FICentre National de la Recherche Scientifique · FRUniversity of Pennsylvania · US

Funding

Structural-Functional Basis of Actin Cytoskeleton DynamicsR01GM073791 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DOMINGUEZ, ROBERTO · 2005 to 2025
$7.0M
NIGMS NIH HHS R01 GM073791
6 · The paper itself

Abstract

ADF/cofilins drive cytoskeletal dynamics by promoting the disassembly of "aged" ADP-actin filaments. Mammals express several ADF/cofilin isoforms, but their specific biochemical activities and cellular functions have not been studied in detail. Here, we demonstrate that the muscle-specific isoform cofilin-2 promotes actin filament disassembly in sarcomeres to control the precise length of thin filaments in the contractile apparatus. In contrast to other isoforms, cofilin-2 efficiently binds and disassembles both ADP- and ATP/ADP-Pi-actin filaments. We mapped surface-exposed cofilin-2-specific residues required for ATP-actin binding and propose that these residues function as an "actin nucleotide-state sensor" among ADF/cofilins. The results suggest that cofilin-2 evolved specific biochemical and cellular properties that allow it to control actin dynamics in sarcomeres, where filament pointed ends may contain a mixture of ADP- and ATP/ADP-Pi-actin subunits. Our findings also offer a rationale for why cofilin-2 mutations in humans lead to myopathies.

Indexed as

Actin CytoskeletonActinsAdenosine DiphosphateAdenosine TriphosphateAmino Acid SequenceAnimalsCells, CulturedCofilin 1Cofilin 2Molecular Sequence DataMuscle ContractionMyocytes, CardiacProtein BindingRatsRNA InterferenceRNA, Small InterferingActinsAdenosine DiphosphateAdenosine TriphosphateADP-G-actinATP-G-actinCofilin 1Cofilin 2RNA, Small Interfering

Identifiers

PMID25373779
PMCPMC4223631
OpenAlexW2009108951

What OpenQuestion holds

Textmetadata
LicenceTDM
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.