Evidence map›Paper›PMID 35930643›Full record

ArticleScience advances2022

The membrane-actin linker ezrin acts as a sliding anchor.

Elgin Korkmazhan, Alexander R Dunn

Abstract read
In one paragraph

Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. ERM Inhibition Confers Ferroptosis Resistance through ROS-Induced NRF2 Signaling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
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  10. Review
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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

2 authors.

Elgin KorkmazhanDepartment of Chemical Engineering, Stanford University, Stanford, CA 94305 USA.ORCID 0000-0002-6872-9952
Alexander R DunnDepartment of Chemical Engineering, Stanford University, Stanford, CA 94305 USA.ORCID 0000-0001-6096-4600

Funding

Molecular mechanisms underlying force transduction at cellular adhesion complexesR35GM130332 · NIGMS · STANFORD UNIVERSITY · PI Alexander R Dunn · 2019 to 2026
$4.9M
NIGMS NIH HHS R35 GM130332
6 · The paper itself

Abstract

Protein linkages to filamentous (F)-actin provide the cell membrane with mechanical stability and support intricate membrane architectures. However, the actin cytoskeleton is highly dynamic and undergoes rapid changes in shape during cell motility and other processes. The molecular mechanisms that generate a mechanically robust yet fluid connection between the membrane and actin cytoskeleton remain poorly understood. Here, we adapted a single-molecule optical trap assay to examine how the prototypical membrane-actin linker ezrin acts to anchor F-actin to the cell membrane. We find that ezrin forms a complex that slides along F-actin over micrometer distances while resisting detachment by forces oriented perpendicular to the filament axis. The ubiquity of ezrin and analogous proteins suggests that sliding anchors such as ezrin may constitute an important but overlooked element in the construction of the actin cytoskeleton.

Identifiers

PMID35930643
PMCPMC9355349

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Registered trials

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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.