Evidence map›Paper›PMID 26952981›Full record

ArticleDevelopment (Cambridge, England)2016

α-Spectrin and integrins act together to regulate actomyosin and columnarization, and to maintain a monolayered follicular epithelium.

Bing Fu Ng, Gokul Kannan Selvaraj, Carmen Santa-Cruz Mateos, Inna Grosheva, Ines Alvarez-Garcia, María Dolores Martín-Bermudo, Isabel M Palacios

Open access · hybridAbstract read
In one paragraph

Article in Development (Cambridge, England), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
  6. Article
  7. The role of integrins inDevelopment (Cambridge, England) · 2019
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. 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

7 authors at 2 institutions in 2 countries.

Bing Fu NgDepartment of Zoology, University of Cambridge, Downing Street, Cambridge CB2 3EJ, UK.
Gokul Kannan SelvarajDepartment of Zoology, University of Cambridge, Downing Street, Cambridge CB2 3EJ, UK.
Carmen Santa-Cruz MateosCentro Andaluz de Biología del Desarrollo CSIC-Univ. Pablo de Olavide, Sevilla 41013, Spain.
Inna GroshevaCentro Andaluz de Biología del Desarrollo CSIC-Univ. Pablo de Olavide, Sevilla 41013, Spain.
Ines Alvarez-GarciaDepartment of Zoology, University of Cambridge, Downing Street, Cambridge CB2 3EJ, UK.
María Dolores Martín-BermudoCentro Andaluz de Biología del Desarrollo CSIC-Univ. Pablo de Olavide, Sevilla 41013, Spain.
Isabel M PalaciosDepartment of Zoology, University of Cambridge, Downing Street, Cambridge CB2 3EJ, UK mip22@cam.ac.uk.
University of Cambridge · GBCentro Andaluz de Biología del Desarrollo · ES

Funding

Biotechnology and Biological Sciences Research Council BB/L001748/1Biotechnology and Biological Sciences Research Council RG42522Wellcome TrustWellcome Trust 087899/Z/08/Z
6 · The paper itself

Abstract

The spectrin cytoskeleton crosslinks actin to the membrane, and although it has been greatly studied in erythrocytes, much is unknown about its function in epithelia. We have studied the role of spectrins during epithelia morphogenesis using the Drosophila follicular epithelium (FE). As previously described, we show that α-Spectrin and β-Spectrin are essential to maintain a monolayered FE, but, contrary to previous work, spectrins are not required to control proliferation. Furthermore, spectrin mutant cells show differentiation and polarity defects only in the ectopic layers of stratified epithelia, similar to integrin mutants. Our results identify α-Spectrin and integrins as novel regulators of apical constriction-independent cell elongation, as α-Spectrin and integrin mutant cells fail to columnarize. Finally, we show that increasing and reducing the activity of the Rho1-Myosin II pathway enhances and decreases multilayering of α-Spectrin cells, respectively. Similarly, higher Myosin II activity enhances the integrin multilayering phenotype. This work identifies a primary role for α-Spectrin in controlling cell shape, perhaps by modulating actomyosin. In summary, we suggest that a functional spectrin-integrin complex is essential to balance adequate forces, in order to maintain a monolayered epithelium.

Indexed as

ActomyosinAnimalsCell DifferentiationCell PolarityCell ShapeCytoskeletonDrosophilaDrosophila ProteinsEpitheliumFemaleIntegrinsMitosisMutationOocytesOvarian FollicleSpectrinActomyosinDrosophila ProteinsIntegrinsSpectrinCell shapeEpitheliumMonolayerProliferationTissue architectureTumor-like mass

Identifiers

PMID26952981
PMCPMC4852512
OpenAlexW2329287555

What OpenQuestion 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 OpenQuestion graph.