Evidence map›Paper›PMID 10385528›Full record

ArticleThe Journal of cell biology1999

Direct involvement of ezrin/radixin/moesin (ERM)-binding membrane proteins in the organization of microvilli in collaboration with activated ERM proteins.

S Yonemura, S Tsukita, S Tsukita

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
5.0field-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

87 citing papers in PubMed, 209 citations in OpenAlex.

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  11. Oocyte ERM and EWI Proteins Are Involved in Mouse Fertilization.Frontiers in cell and developmental biology · 2022
    Article
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  18. (Patho-)Physiology of NaFrontiers in physiology · 2019
    Review
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  20. Article

27 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 2 institutions in 1 country.

S YonemuraDepartment of Cell Biology, Faculty of Medicine, Kyoto University, Kyoto 606-8501, Japan. yonemura@mfour.med.kyoto-u.ac.jp
S Tsukita
S Tsukita
Kyoto University · JPKyoto College of Medical Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ezrin/radixin/moesin (ERM) proteins have been thought to play a central role in the organization of cortical actin-based cytoskeletons including microvillar formation through cross-linking actin filaments and integral membrane proteins such as CD43, CD44, and ICAM-2. To examine the functions of these ERM-binding membrane proteins (ERMBMPs) in cortical morphogenesis, we overexpressed ERMBMPs (the extracellular domain of E-cadherin fused with the transmembrane/cytoplasmic domain of CD43, CD44, or ICAM-2) in various cultured cells. In cultured fibroblasts such as L and CV-1 cells, their overexpression significantly induced microvillar elongation, recruiting ERM proteins and actin filaments. When the ERM-binding domains were truncated from these molecules, their ability to induce microvillar elongation became undetectable. In contrast, in cultured epithelial cells such as MTD-1A and A431 cells, the overexpression of ERMBMPs did not elongate microvilli. However, in the presence of EGF, overexpression of ERMBMPs induced remarkable microvillar elongation in A431 cells. These results indicated that ERMBMPs function as organizing centers for cortical morphogenesis by organizing microvilli in collaboration with activated ERM proteins. Furthermore, immunodetection with a phosphorylated ERM-specific antibody and site-directed mutagenesis suggested that ERM proteins phosphorylated at their COOH-terminal threonine residue represent activated ERM proteins.

Indexed as

Cytoskeletal ProteinsActin CytoskeletonActinsAnimalsAntigens, CDBlood ProteinsCadherinsCell Adhesion MoleculesCell LineEpidermal Growth FactorEpithelial CellsEzrinFibroblastsHumansHyaluronan ReceptorsLeukosialinActinsAntigens, CDBlood ProteinsCadherinsCell Adhesion MoleculesCytoskeletal ProteinsEpidermal Growth FactorEzrinHyaluronan ReceptorsICAM2 protein, humanLeukosialinMembrane ProteinsMicrofilament ProteinsmoesinPhosphoproteinsradixinRecombinant Fusion ProteinsSialoglycoproteinsSPN protein, humanThreonine

Identifiers

PMID10385528
PMCPMC2133160
OpenAlexW2078539894

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.