Evidence map›Paper›PMID 12213838›Full record

ArticleThe Journal of cell biology2002

Crumbs interacts with moesin and beta(Heavy)-spectrin in the apical membrane skeleton of Drosophila.

Emmanuelle Médina, Janice Williams, Elizabeth Klipfell, Daniela Zarnescu, Claire M. Thomas, André Le Bivic

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
3.3field-weighted citation impact, top 9% 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

83 citing papers in PubMed, 186 citations in OpenAlex.

  1. Opposing Activity at the Apical Surface: An Antagonistic Collaboration Between Crumbs and Myosin II Determines Organ Shape.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  2. Article
  3. The Life of a Kidney Podocyte.Acta physiologica (Oxford, England) · 2025
    Review
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23 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

6 authors at 2 institutions in 2 countries.

Emmanuelle MédinaLaboratoire de Neurogenèse et Morphogenèse dans le Développement et l'Adulte, Institut de Biologie du Développement de Marseille, Université de la Méditerranée, 13288 Marseille, cedex 09, France.
Janice Williams
Elizabeth Klipfell
Daniela Zarnescu
Claire M. Thomas
André Le Bivic
Pennsylvania State University · USInstitut de Biologie du Développement Marseille · FR

Funding

BETA H-SPECTRIN--ROLES IN CELL POLARITY AND SIGNALINGR01GM052506 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI THOMAS, GRAHAM H · 1997 to 2001
$337k
ANALYSIS OF ZONULA ADHERENS DEFECTS IN SPECTRIN MUTANTSF31GM020906 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI WILLIAMS, JANICE A · 2000 to 2003
$104k
NIGMS NIH HHS F31 GM020906NIGMS NIH HHS GM20906NIGMS NIH HHS GM 52506
6 · The paper itself

Abstract

The apical transmembrane protein Crumbs is necessary for both cell polarization and the assembly of the zonula adherens (ZA) in Drosophila epithelia. The apical spectrin-based membrane skeleton (SBMS) is a protein network that is essential for epithelial morphogenesis and ZA integrity, and exhibits close colocalization with Crumbs and the ZA in fly epithelia. These observations suggest that Crumbs may stabilize the ZA by recruiting the SBMS to the junctional region. Consistent with this hypothesis, we report that Crumbs is necessary for the organization of the apical SBMS in embryos and Schneider 2 cells, whereas the localization of Crumbs is not affected in karst mutants that eliminate the apical SBMS. Our data indicate that it is specifically the 4.1 protein/ezrin/radixin/moesin (FERM) domain binding consensus, and in particular, an arginine at position 7 in the cytoplasmic tail of Crumbs that is essential to efficiently recruit both the apical SBMS and the FERM domain protein, DMoesin. Crumbs, Discs lost, betaHeavy-spectrin, and DMoesin are all coimmunoprecipitated from embryos, confirming the existence of a multimolecular complex. We propose that Crumbs stabilizes the apical SBMS via DMoesin and actin, leading to reinforcement of the ZA and effectively coupling epithelial morphogenesis and cell polarity.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCell MembraneCell PolarityCytoplasmCytoskeletonDrosophilaDrosophila ProteinsInsect ProteinsMacromolecular SubstancesMembrane ProteinsModels, BiologicalMolecular Sequence DataProtein BindingProtein Structure, Tertiarycrb protein, Drosophiladlt protein, DrosophilaDrosophila ProteinsInsect Proteinskst protein, DrosophilaMacromolecular SubstancesMembrane Proteinsmoesin, DrosophilaRecombinant ProteinsSpectrin

Identifiers

PMID12213838
PMCPMC2173152
OpenAlexW1984768151

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.