Evidence map›Paper›PMID 33740033›Full record

ArticleThe Journal of cell biology2021

Stochastic combinations of actin regulatory proteins are sufficient to drive filopodia formation.

Ulrich Dobramysl, Iris Katharina Jarsch, Yoshiko Inoue, Hanae Shimo, Benjamin Richier, Jonathan R Gadsby, Julia Mason, Alicja Szałapak, Pantelis Savvas Ioannou, Guilherme Pereira Correia and 5 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

18 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Chiral growth of adherent filopodia.Biophysical journal · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Functions of Arp2/3 Complex in the Dynamics of Epithelial Tissues.Frontiers in cell and developmental biology · 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

15 authors at 2 institutions in 2 countries.

Ulrich Dobramysl *Gurdon Institute, University of Cambridge, Cambridge, UK.
Iris Katharina Jarsch *Gurdon Institute, University of Cambridge, Cambridge, UK.
Yoshiko Inoue *Gurdon Institute, University of Cambridge, Cambridge, UK.
Hanae Shimo *Gurdon Institute, University of Cambridge, Cambridge, UK.
Benjamin RichierGurdon Institute, University of Cambridge, Cambridge, UK.
Jonathan R GadsbyGurdon Institute, University of Cambridge, Cambridge, UK.
Julia MasonGurdon Institute, University of Cambridge, Cambridge, UK.
Alicja SzałapakGurdon Institute, University of Cambridge, Cambridge, UK.
Pantelis Savvas IoannouGurdon Institute, University of Cambridge, Cambridge, UK.
Guilherme Pereira CorreiaGurdon Institute, University of Cambridge, Cambridge, UK.
Astrid WalrantGurdon Institute, University of Cambridge, Cambridge, UK.
Richard ButlerGurdon Institute, University of Cambridge, Cambridge, UK.
Edouard HannezoGurdon Institute, University of Cambridge, Cambridge, UK.
Benjamin D SimonsGurdon Institute, University of Cambridge, Cambridge, UK.
Jennifer L GallopGurdon Institute, University of Cambridge, Cambridge, UK.
University of Cambridge · GBInstitute of Science and Technology Austria · AT

Funding

Austrian Science Fund FWF P 31639Cancer Research UK C6946/A14492European Research Council 281971Medical Research Council MC_PC_17230Wellcome Trust 092096Wellcome Trust 098357Wellcome Trust 105602/Z/14/ZWellcome Trust 219482/Z/19/ZWellcome Trust WT095829AIA
6 · The paper itself

Abstract

Assemblies of actin and its regulators underlie the dynamic morphology of all eukaryotic cells. To understand how actin regulatory proteins work together to generate actin-rich structures such as filopodia, we analyzed the localization of diverse actin regulators within filopodia in Drosophila embryos and in a complementary in vitro system of filopodia-like structures (FLSs). We found that the composition of the regulatory protein complex where actin is incorporated (the filopodial tip complex) is remarkably heterogeneous both in vivo and in vitro. Our data reveal that different pairs of proteins correlate with each other and with actin bundle length, suggesting the presence of functional subcomplexes. This is consistent with a theoretical framework where three or more redundant subcomplexes join the tip complex stochastically, with any two being sufficient to drive filopodia formation. We provide an explanation for the observed heterogeneity and suggest that a mechanism based on multiple components allows stereotypical filopodial dynamics to arise from diverse upstream signaling pathways.

Indexed as

AnimalsDrosophila melanogasterDrosophila ProteinsEmbryo, NonmammalianFatty Acid-Binding ProteinsPseudopodiaXenopusXenopus ProteinsDrosophila ProteinsFatty Acid-Binding ProteinsFNBP1L protein, XenopusXenopus Proteins

Identifiers

PMID33740033
PMCPMC7980258
OpenAlexW3139472095

What OpenQuestion holds

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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.