Evidence map›Paper›PMID 31018575›Full record

ReviewInternational journal of molecular sciences2019

Two Sides of the Coin: Ezrin/Radixin/Moesin and Merlin Control Membrane Structure and Contact Inhibition.

Katharine A Michie, Adam Bermeister, Neil O Robertson, Sophia C Goodchild, Paul M G Curmi

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

43 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
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  4. Review
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  11. Translational cancer research · 2024
    Article
  12. Article
  13. A bipartite NLS motif mediates the nuclear import ofFrontiers in cell and developmental biology · 2024
    Article
  14. Article
  15. Inherited human ezrin deficiency impairs adaptive immunity.The Journal of allergy and clinical immunology · 2023
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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 2 institutions in 1 country.

Katharine A MichieSchool of Physics, University of New South Wales, Sydney 2052, Australia. k.michie@unsw.edu.au.ORCID 0000-0002-2133-2237
Adam BermeisterSchool of Physics, University of New South Wales, Sydney 2052, Australia. adam.bermeister@gmail.com.
Neil O RobertsonSchool of Physics, University of New South Wales, Sydney 2052, Australia. robertn1@mskcc.org.
Sophia C GoodchildDepartment of Molecular Sciences, Macquarie University, Sydney 2109, Australia. sophia.goodchild@mq.edu.au.
Paul M G CurmiSchool of Physics, University of New South Wales, Sydney 2052, Australia. p.curmi@unsw.edu.au.ORCID 0000-0001-5762-7638
UNSW Sydney · AUMacquarie University · AU

Funding

National Health and Medical Research Council APP1085718
6 · The paper itself

Abstract

The merlin-ERM (ezrin, radixin, moesin) family of proteins plays a central role in linking the cellular membranes to the cortical actin cytoskeleton. Merlin regulates contact inhibition and is an integral part of cell-cell junctions, while ERM proteins, ezrin, radixin and moesin, assist in the formation and maintenance of specialized plasma membrane structures and membrane vesicle structures. These two protein families share a common evolutionary history, having arisen and separated via gene duplication near the origin of metazoa. During approximately 0.5 billion years of evolution, the merlin and ERM family proteins have maintained both sequence and structural conservation to an extraordinary level. Comparing crystal structures of merlin-ERM proteins and their complexes, a picture emerges of the merlin-ERM proteins acting as switchable interaction hubs, assembling protein complexes on cellular membranes and linking them to the actin cytoskeleton. Given the high level of structural conservation between the merlin and ERM family proteins we speculate that they may function together.

Indexed as

Actin CytoskeletonAmino Acid SequenceAnimalsCell MembraneContact InhibitionCytoskeletal ProteinsEzrinHumansMembrane ProteinsMicrofilament ProteinsModels, MolecularNeurofibromin 2Protein ConformationProtein DomainsProtein Interaction MapsSequence AlignmentCytoskeletal ProteinsEzrinMembrane ProteinsMicrofilament ProteinsmoesinNeurofibromin 2radixinezrinFERM domainmerlinmoesinradixin

Identifiers

PMID31018575
PMCPMC6515277
OpenAlexW2942019407

What Socratic 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 Socratic graph.