Evidence map›Paper›PMID 8522586›Full record

ArticleThe Journal of cell biology1995

Ezrin oligomers are major cytoskeletal components of placental microvilli: a proposal for their involvement in cortical morphogenesis.

M Berryman, R Gary, A Bretscher

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
15.5field-weighted citation impact, top 1% 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

64 citing papers in PubMed, 210 citations in OpenAlex.

  1. On the mechanism of ezrin activation.Biophysical journal · 2026
    Article
  2. On the Mechanism of Ezrin Activation.bioRxiv : the preprint server for biology · 2025
    Article
  3. The Molecular Biology of Placental Transport of Calcium to the Human Foetus.International journal of molecular sciences · 2025
    Review
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4 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

M BerrymanSection of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853, USA.
R Gary
A Bretscher
Cornell University · US

Funding

MICROFILAMENT ORGANIZATION AND REGULATIONR01GM036652 · NIGMS · CORNELL UNIVERSITY ITHACA · PI BRETSCHER, ANTHONY P. · 1986 to 2018
$8.7M
EZRIN PHOSPHORYLATION AND FUNCTION IN MEMBRANE RUFFLINGF32GM014352 · NIGMS · CORNELL UNIVERSITY ITHACA · PI BERRYMAN, MARK ALAN · 1991 to 1993
–
NIGMS NIH HHS GM14352NIGMS NIH HHS GM36652
6 · The paper itself

Abstract

Ezrin is a component of the microvillus cytoskeleton of a variety of polarized epithelial cells and is believed to function as a membrane-cytoskeletal linker. In this study, we isolated microvilli from human placental syncytiotrophoblast as a model system for biochemical analysis of ezrin function. In contrast to intestinal microvilli, ezrin is a major protein component of placental microvilli, comprising approximately 5% of the total protein mass and present at about one quarter of the molar abundance of actin. Gel filtration and chemical cross-linking studies demonstrated that ezrin exists mainly in the form of noncovalent dimers and higher order oligomers in extracts of placental microvilli. A novel form of ezrin, apparently representing covalently cross-linked adducts, was present as a relatively minor constituent of placental microvilli. Both oligomers and adducts remained associated with the detergent-insoluble cytoskeleton, indicating a tight interaction with actin filaments. Moreover, stimulation of human A431 carcinoma cells with EGF induces the rapid formation of ezrin oligomers in vivo, thus identifying a signal transduction pathway involving ezrin oligomerization coincident with microvillus assembly. In addition to time course studies, experiments with tyrosine kinase and tyrosine phosphatase inhibitors revealed a correlation between the phosphorylation of ezrin on tyrosine and the onset of oligomer formation, consistent with the possibility that phosphorylation of ezrin might be required for the generation of stable oligomers. Based on these observations, a model for the assembly of cell surface structures is proposed.

Indexed as

AnimalsCytoskeletal ProteinsCytoskeletonDetergentsEpidermal Growth FactorEzrinHumansMiceMicrovilliMorphogenesisOctoxynolPhosphoproteinsPhosphorylationPlacentaPlacentationSolubilityCytoskeletal ProteinsDetergentsEpidermal Growth FactorEzrinOctoxynolPhosphoproteinsTyrosine

Identifiers

PMID8522586
PMCPMC2120629
OpenAlexW2051384784

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.