Evidence map›Paper›PMID 34525374›Full record

ArticleCell reports2021

Myosin-X and talin modulate integrin activity at filopodia tips.

Mitro Miihkinen, Max L B Grönloh, Ana Popović, Helena Vihinen, Eija Jokitalo, Benjamin T Goult, Johanna Ivaska, Guillaume Jacquemet

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
5.2field-weighted citation impact, top 3% 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

29 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
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  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Modulation of Filopodial Myosin Function.bioRxiv : the preprint server for biology · 2025
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  10. Article
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  15. Article
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  17. Chiral growth of adherent filopodia.Biophysical journal · 2023
    Article
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  20. 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

8 authors at 3 institutions in 2 countries.

Mitro MiihkinenTurku Bioscience Centre, University of Turku and Åbo Akademi University, 20520 Turku, Finland.
Max L B GrönlohTurku Bioscience Centre, University of Turku and Åbo Akademi University, 20520 Turku, Finland.
Ana PopovićTurku Bioscience Centre, University of Turku and Åbo Akademi University, 20520 Turku, Finland; Faculty of Science and Engineering, Cell Biology, Åbo Akademi University, 20520 Turku, Finland.
Helena VihinenElectron Microscopy Unit, Institute of Biotechnology, University of Helsinki, 00790 Helsinki, Finland.
Eija JokitaloElectron Microscopy Unit, Institute of Biotechnology, University of Helsinki, 00790 Helsinki, Finland.
Benjamin T GoultSchool of Biosciences, University of Kent, Canterbury, CT2 7NJ Kent, UK.
Johanna IvaskaTurku Bioscience Centre, University of Turku and Åbo Akademi University, 20520 Turku, Finland; Department of Life Technologies, University of Turku, 20520 Turku, Finland; InFLAMES Research Flagship Center, University of Turku, 20520 Turku, Finland. Electronic address: johanna.ivaska@utu.fi.
Guillaume JacquemetTurku Bioscience Centre, University of Turku and Åbo Akademi University, 20520 Turku, Finland; Faculty of Science and Engineering, Cell Biology, Åbo Akademi University, 20520 Turku, Finland; Turku Bioimaging, University of Turku and Åbo Akademi University, 20520 Turku, Finland. Electronic address: guillaume.jacquemet@abo.fi.
Åbo Akademi University · FIUniversity of Helsinki · FIUniversity of Kent · GB

Funding

Biotechnology and Biological Sciences Research Council BB/N007336/1
6 · The paper itself

Abstract

Filopodia assemble unique integrin-adhesion complexes to sense the extracellular matrix. However, the mechanisms of integrin regulation in filopodia are poorly defined. Here, we report that active integrins accumulate at the tip of myosin-X (MYO10)-positive filopodia, while inactive integrins are uniformly distributed. We identify talin and MYO10 as the principal integrin activators in filopodia. In addition, deletion of MYO10's FERM domain, or mutation of its β1-integrin-binding residues, reveals MYO10 as facilitating integrin activation, but not transport, in filopodia. However, MYO10's isolated FERM domain alone cannot activate integrins, potentially because of binding to both integrin tails. Finally, because a chimera construct generated by swapping MYO10-FERM by talin-FERM enables integrin activation in filopodia, our data indicate that an integrin-binding FERM domain coupled to a myosin motor is a core requirement for integrin activation in filopodia. Therefore, we propose a two-step integrin activation model in filopodia: receptor tethering by MYO10 followed by talin-mediated integrin activation.

Indexed as

Binding SitesCell Line, TumorFocal AdhesionsHumansIntegrin beta1MyosinsProtein BindingProtein DomainsPseudopodiaRNA InterferenceRNA, Small InterferingTalinIntegrin beta1MYO10 protein, humanMyosinsRNA, Small InterferingTalinadhesionFilopodiaintegrin activityMYO10talin

Identifiers

PMID34525374
PMCPMC8456781
OpenAlexW3199134013

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.