Evidence map›Paper›PMID 38193818›Full record

ArticleeLife2024

ARHGAP18-ezrin functions as an autoregulatory module for RhoA in the assembly of distinct actin-based structures.

Andrew T Lombardo, Cameron A R Mitchell, Riasat Zaman, David J McDermitt, Anthony Bretscher

Open access · goldAbstract read
In one paragraph

Article in eLife, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

14 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. On the mechanism of ezrin activation.Biophysical journal · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. On the Mechanism of Ezrin Activation.bioRxiv : the preprint server for biology · 2025
    Article
  8. Article
  9. Myosin 2 - A general contractor for the cytoskeleton.Current opinion in cell biology · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024
    Review
  14. 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

5 authors at 1 institution in 1 country.

Andrew T LombardoDepartment of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, United States.ORCID https://orcid.org/0000-0002-1814-5748
Cameron A R MitchellDepartment of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, United States.
Riasat ZamanDepartment of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, United States.
David J McDermittDepartment of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, United States.
Anthony BretscherDepartment of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, United States.ORCID https://orcid.org/0000-0002-1122-8970
Cornell University · US

Funding

Microfilament Function in Cell PolarityR35GM131751 · NIGMS · CORNELL UNIVERSITY · PI BRETSCHER, ANTHONY P. · 2019 to 2022
$3.2M
NIGMS NIH HHS R35 GM131751NIGMS NIH HHS R35GM131751
6 · The paper itself

Abstract

The location of different actin-based structures is largely regulated by Rho GTPases through specific effectors. We use the apical aspect of epithelial cells as a model system to investigate how RhoA is locally regulated to contribute to two distinct adjacent actin-based structures. Assembly of the non-muscle myosin-2 filaments in the terminal web is dependent on RhoA activity, and assembly of the microvilli also requires active RhoA for phosphorylation and activation of ezrin. We show that the RhoGAP, ARHGAP18, is localized by binding active microvillar ezrin, and this interaction enhances ARHGAP18's RhoGAP activity. We present a model where ezrin-ARHGAP18 acts as a negative autoregulatory module to locally reduce RhoA activity in microvilli. Consistent with this model, loss of ARHGAP18 results in disruption of the distinction between microvilli and the terminal web including aberrant assembly of myosin-2 filaments forming inside microvilli. Thus, ARHGAP18, through its recruitment and activation by ezrin, fine-tunes the local level of RhoA to allow for the appropriate distribution of actin-based structures between the microvilli and terminal web. As RhoGAPs vastly outnumber Rho GTPases, this may represent a general mechanism whereby individual Rho effectors drive specific actin-based structures.

Indexed as

ActinsCytoskeletal ProteinsEzrinMyosinsrho GTP-Binding ProteinsActinsCytoskeletal ProteinsEzrinMyosinsrho GTP-Binding Proteinsactincell biologyezrinhumanmicrovillipolarityRho GAP

Identifiers

PMID38193818
PMCPMC10830128
OpenAlexW4390758263

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.