Evidence map›Paper›PMID 38514695›Full record

ArticleNature communications2024

Focal adhesions contain three specialized actin nanoscale layers.

Reena Kumari, Katharina Ven, Megan Chastney, Shrikant B Kokate, Johan Peränen, Jesse Aaron, Konstantin Kogan, Leonardo Almeida-Souza, Elena Kremneva, Renaud Poincloux and 4 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
16.3field-weighted citation impact, top 1% 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

36 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
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  4. Review
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  7. Synergistic effect of PIPBiophysical journal · 2026
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  13. Mechanically-induced Septin Networks Protect Nuclear Integrity.bioRxiv : the preprint server for biology · 2026
    Article
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  15. Article
  16. Review
  17. Article
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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

14 authors at 5 institutions in 4 countries.

Reena KumariHiLIFE Institute of Biotechnology, University of Helsinki, FI-00014, Helsinki, Finland.
Katharina VenHiLIFE Institute of Biotechnology, University of Helsinki, FI-00014, Helsinki, Finland.
Megan ChastneyTurku Bioscience Centre, University of Turku and Åbo Akademi University, FI-20520, Turku, Finland.ORCID http://orcid.org/0000-0002-9866-2322
Shrikant B KokateHiLIFE Institute of Biotechnology, University of Helsinki, FI-00014, Helsinki, Finland.ORCID http://orcid.org/0000-0002-6274-537X
Johan PeränenHiLIFE Institute of Biotechnology, University of Helsinki, FI-00014, Helsinki, Finland.
Jesse AaronAdvanced Imaging Center, HHMI Janelia Research Campus, Ashburn, VA, 20147, USA.ORCID http://orcid.org/0000-0002-7543-9590
Konstantin KoganHiLIFE Institute of Biotechnology, University of Helsinki, FI-00014, Helsinki, Finland.ORCID http://orcid.org/0000-0003-3270-9391
Leonardo Almeida-SouzaHiLIFE Institute of Biotechnology, University of Helsinki, FI-00014, Helsinki, Finland.
Elena KremnevaHiLIFE Institute of Biotechnology, University of Helsinki, FI-00014, Helsinki, Finland.
Renaud PoinclouxInstitut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, UPS, Toulouse, France.ORCID http://orcid.org/0000-0003-2884-1744
Teng-Leong ChewAdvanced Imaging Center, HHMI Janelia Research Campus, Ashburn, VA, 20147, USA.ORCID http://orcid.org/0000-0002-3139-7560
Peter W GunningSchool of Biomedical Sciences, UNSW Sydney, Wallace Wurth Building, Sydney, NSW 2052, Australia.ORCID http://orcid.org/0000-0003-0833-3128
Johanna IvaskaTurku Bioscience Centre, University of Turku and Åbo Akademi University, FI-20520, Turku, Finland.ORCID http://orcid.org/0000-0002-6802-6739
Pekka LappalainenHiLIFE Institute of Biotechnology, University of Helsinki, FI-00014, Helsinki, Finland. pekka.lappalainen@helsinki.fi.ORCID http://orcid.org/0000-0001-6227-0354
University of Helsinki · FIÅbo Akademi University · FIJanelia Research Campus · USCentre National de la Recherche Scientifique · FRUNSW Sydney · AU

Funding

Academy of Finland (Suomen Akatemia) 346133
6 · The paper itself

Abstract

Focal adhesions (FAs) connect inner workings of cell to the extracellular matrix to control cell adhesion, migration and mechanosensing. Previous studies demonstrated that FAs contain three vertical layers, which connect extracellular matrix to the cytoskeleton. By using super-resolution iPALM microscopy, we identify two additional nanoscale layers within FAs, specified by actin filaments bound to tropomyosin isoforms Tpm1.6 and Tpm3.2. The Tpm1.6-actin filaments, beneath the previously identified α-actinin cross-linked actin filaments, appear critical for adhesion maturation and controlled cell motility, whereas the adjacent Tpm3.2-actin filament layer beneath seems to facilitate adhesion disassembly. Mechanistically, Tpm3.2 stabilizes ACF-7/MACF1 and KANK-family proteins at adhesions, and hence targets microtubule plus-ends to FAs to catalyse their disassembly. Tpm3.2 depletion leads to disorganized microtubule network, abnormally stable FAs, and defects in tail retraction during migration. Thus, FAs are composed of distinct actin filament layers, and each may have specific roles in coupling adhesions to the cytoskeleton, or in controlling adhesion dynamics.

Indexed as

ActinsFocal AdhesionsActin CytoskeletonCytoskeletonProtein IsoformsActinsProtein Isoforms

Identifiers

PMID38514695
PMCPMC10957975
OpenAlexW4393032128

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.