Evidence map›Paper›PMID 24461009›Full record

ArticleBiophysical journal2014

Quantitative analysis of ezrin turnover dynamics in the actin cortex.

Marco Fritzsche, Richard Thorogate, Guillaume Charras

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

35 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. On the mechanism of ezrin activation.Biophysical journal · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. On the Mechanism of Ezrin Activation.bioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Article
  9. A bipartite NLS motif mediates the nuclear import ofFrontiers in cell and developmental biology · 2024
    Article
  10. Modeling the dynamics of actin and myosin during bleb stabilization.bioRxiv : the preprint server for biology · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
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  20. Article
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

3 authors at 2 institutions in 1 country.

Marco FritzscheDepartment of Physics and Astronomy, University College London, London, United Kingdom; London Centre for Nanotechnology, University College London, London, United Kingdom.
Richard ThorogateLondon Centre for Nanotechnology, University College London, London, United Kingdom.
Guillaume CharrasLondon Centre for Nanotechnology, University College London, London, United Kingdom; Department of Cell and Developmental Biology, University College London, London, United Kingdom. Electronic address: g.charras@ucl.ac.uk.
London Centre for Nanotechnology · GBUniversity College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F019769/1Biotechnology and Biological Sciences Research Council BB/F021402Biotechnology and Biological Sciences Research Council BB/F021402/1
6 · The paper itself

Abstract

Proteins of the ERM family (ezrin, moesin, radixin) play a fundamental role in tethering the membrane to the cellular actin cortex as well as regulating cortical organization and mechanics. Overexpression of dominant inactive forms of ezrin leads to fragilization of the membrane-cortex link and depletion of moesin results in softer cortices that disrupt spindle orientation during cytokinesis. Therefore, the kinetics of association of ERM proteins with the cortex likely influence the timescale of cortical signaling events and the dynamics of membrane interfacing to the cortex. However, little is known about ERM protein turnover at the membrane-cortex interface. Here, we examined cortical ezrin dynamics using fluorescence recovery after photobleaching experiments and single-molecule imaging. Using multiexponential fitting of fluorescence recovery curves, we showed that ezrin turnover resulted from three molecular mechanisms acting on very different timescales. The fastest turnover process was due to association/dissociation from the F-actin cortex, suggesting that ezrin acts as a link that leads to low friction between the membrane and the cortex. The second turnover process resulted from association/dissociation of ezrin from the membrane and the slowest turnover process resulted from the slow diffusion of ezrin in the plane of the membrane. In summary, ezrin-mediated membrane-cortex tethering resulted from long-lived interactions with the membrane via the FERM domain coupled with shorter-lived interactions with the cortex. The slow diffusion of membranous ezrin and its interaction partners relative to the cortex signified that signals emanating from membrane-associated ezrin may locally act to modulate cortical organization and contractility.

Indexed as

ActinsCell Line, TumorCell MembraneCytoskeletal ProteinsDiffusionEzrinFluorescence Resonance Energy TransferHumansKineticsMolecular ImagingPoint MutationProtein StabilityActinsCytoskeletal ProteinsEzrin

Identifiers

PMID24461009
PMCPMC3907236
OpenAlexW1982773983

What OpenQuestion holds

Textmetadata
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.