Evidence map›Paper›PMID 27926869›Full record

ArticleCell reports2016

Robust Asymmetric Localization of Planar Polarity Proteins Is Associated with Organization into Signalosome-like Domains of Variable Stoichiometry.

Helen Strutt, Jessica Gamage, David Strutt

Abstract read
In one paragraph

Article in Cell reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
–field-weighted citation impact
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

41 citing papers in PubMed.

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  15. The origin and evolution of Wnt signalling.Nature reviews. Genetics · 2024
    Review
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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.

Helen StruttBateson Centre, Department of Biomedical Science, University of Sheffield, Western Bank, Sheffield S10 2TN, UK.
Jessica GamageBateson Centre, Department of Biomedical Science, University of Sheffield, Western Bank, Sheffield S10 2TN, UK.
David StruttBateson Centre, Department of Biomedical Science, University of Sheffield, Western Bank, Sheffield S10 2TN, UK. Electronic address: d.strutt@sheffield.ac.uk.

Funding

Medical Research Council G0900203-1/1Medical Research Council G1000405-1/1Wellcome Trust 100986/Z/13/Z
6 · The paper itself

Abstract

In developing epithelia, the core planar polarity proteins physically interact with each other and localize asymmetrically at opposite cell ends, forming intercellular complexes that link the polarity of neighboring cells. Using quantitative imaging to examine the composition of the core protein complex in vivo, we find that complex composition is unexpectedly plastic. The transmembrane proteins Frizzled and Flamingo form a stoichiometric nucleus in the complex, while the relative levels of the other four core proteins can vary independently. Exploring the functional consequences of this, we show that robust cell polarization is achieved over a range of complex stoichiometries but is dependent on maintaining appropriate levels of the components Frizzled and Strabismus. We propose that the core proteins assemble into signalosome-like structures, where stable association is not dependent on one-to-one interactions with binding partners, and signaling functions can act over a wide range of complex compositions.

Indexed as

AnimalsBody PatterningCadherinsCell NucleusCell PolarityDrosophilaDrosophila ProteinsFrizzled ReceptorsMembrane ProteinsProtein BindingCadherinsDrosophila ProteinsFrizzled Receptorsfz protein, DrosophilaMembrane Proteinsstan protein, DrosophilaVang protein, DrosophilafrizzledPCPplanar polaritypolaritysignalingstoichiometry

Identifiers

PMID27926869
PMCPMC5177602

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Registered trials

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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.