Evidence map›Paper›PMID 24151071›Full record

ArticleThe Journal of biological chemistry2013

Interactome analysis reveals ezrin can adopt multiple conformational states.

Raghuvir Viswanatha, Jessica Wayt, Patrice Y Ohouo, Marcus B Smolka, Anthony Bretscher

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.5field-weighted citation impact, top 12% 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

33 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. ERM Inhibition Confers Ferroptosis Resistance through ROS-Induced NRF2 Signaling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  5. Article
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  12. Cotranslational interaction of human EBP50 and ezrin overcomes masked binding site during complex assembly.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Chemokine-biased robust self-organizing polarization of migrating cells in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. Article
  19. Article
  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

5 authors at 1 institution in 1 country.

Raghuvir ViswanathaFrom the Department of Molecular Biology and Genetics and Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, New York 14853.
Jessica Wayt
Patrice Y Ohouo
Marcus B Smolka
Anthony Bretscher
Cornell University · US

Funding

PREDOCTORAL TRAINING IN CELLULAR AND MOLECULAR BIOLOGYT32GM007273 · NIGMS · CORNELL UNIVERSITY ITHACA · PI BRETSCHER, ANTHONY P. · 1985 to 2019
$11.6M
MICROFILAMENT ORGANIZATION AND REGULATIONR01GM036652 · NIGMS · CORNELL UNIVERSITY ITHACA · PI BRETSCHER, ANTHONY P. · 1986 to 2018
$8.7M
Cellular Responses to DNA Replication StressR01GM097272 · NIGMS · CORNELL UNIVERSITY · PI SMOLKA, MARCUS · 2011 to 2020
$2.7M
NIGMS NIH HHS 5T32GM007273NIGMS NIH HHS GM-036652NIGMS NIH HHS R01 GM036652NIGMS NIH HHS R01 GM097272NIGMS NIH HHS T32 GM007273
6 · The paper itself

Abstract

Ezrin, a member of the ezrin-radixin-moesin family (ERM), is an essential regulator of the structure of microvilli on the apical aspect of epithelial cells. Ezrin provides a linkage between membrane-associated proteins and F-actin, oscillating between active/open and inactive/closed states, and is regulated in part by phosphorylation of a C-terminal threonine. In the open state, ezrin can bind a number of ligands, but in the closed state the ligand-binding sites are inaccessible. In vitro analysis has proposed that there may be a third hyperactivated form of ezrin. To gain a better understanding of ezrin, we conducted an unbiased proteomic analysis of ezrin-binding proteins in an epithelial cell line, Jeg-3. We refined our list of interactors by comparing the interactomes using quantitative mass spectrometry between wild-type ezrin, closed ezrin, open ezrin, and hyperactivated ezrin. The analysis reveals several novel interactors confirmed by their localization to microvilli, as well as a significant class of proteins that bind closed ezrin. Taken together, the data indicate that ezrin can exist in three different conformational states, and different ligands "perceive" ezrin conformational states differently.

Indexed as

Amino Acid SubstitutionCell LineCore Binding FactorsCytoskeletal ProteinsEzrinHumansLigandsMass SpectrometryMicrovilliMutagenesis, Site-DirectedPhosphoproteinsPhosphorylationProtein BindingProtein ConformationProtein Structure, TertiaryProteomeCore Binding FactorsCytoskeletal ProteinsEzrinLigandsPhosphoproteinsProteomeRecombinant Proteinssodium-hydrogen exchanger regulatory factorSodium-Hydrogen ExchangersCytoskeletonEzrinPhosphorylationPlasma MembraneProteomics

Identifiers

PMID24151071
PMCPMC3853291
OpenAlexW1982999071

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.