Evidence map›Paper›PMID 28883443›Full record

ArticleNature communications2017

Planar polarized Rab35 functions as an oscillatory ratchet during cell intercalation in the Drosophila epithelium.

Cayla E Jewett, Timothy E Vanderleest, Hui Miao, Yi Xie, Roopa Madhu, Dinah Loerke, J Todd Blankenship

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

40 citing papers in PubMed, 66 citations in OpenAlex.

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  19. A PtdIns(3,4,5)PDevelopmental cell · 2021
    Article
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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

7 authors at 1 institution in 1 country.

Cayla E JewettDepartment of Biological Sciences, University of Denver, Denver, CO, 80208, USA.
Timothy E VanderleestDepartment of Physics, University of Denver, Denver, CO, 80208, USA.
Hui MiaoDepartment of Biological Sciences, University of Denver, Denver, CO, 80208, USA.
Yi XieDepartment of Biological Sciences, University of Denver, Denver, CO, 80208, USA.
Roopa MadhuDepartment of Physics, University of Denver, Denver, CO, 80208, USA.
Dinah LoerkeDepartment of Physics, University of Denver, Denver, CO, 80208, USA. dinah.loerke@du.edu.
J Todd BlankenshipDepartment of Biological Sciences, University of Denver, Denver, CO, 80208, USA. todd.blankenship@du.edu.
University of Denver · US

Funding

Dynamics of Epithelial Polarity Proteins and the Control of Tissue ArchitectureR01GM090065 · NIGMS · UNIVERSITY OF DENVER (COLORADO SEMINARY) · PI BLANKENSHIP, JAMES TODD · 2011 to 2015
$1.4M
Mechanisms of membrane ratcheting during cell intercalationR15GM126422 · NIGMS · UNIVERSITY OF DENVER (COLORADO SEMINARY) · PI BLANKENSHIP, JAMES TODD · 2017 to 2017
$440k
The Biomechanics of Intercalation in Germ-Band ElongationR15GM117463 · NIGMS · UNIVERSITY OF DENVER (COLORADO SEMINARY) · PI LOERKE, DINAH · 2016 to 2016
$438k
NIGMS NIH HHS R01 GM090065NIGMS NIH HHS R15 GM117463NIGMS NIH HHS R15 GM126422
6 · The paper itself

Abstract

The coordination between membrane trafficking and actomyosin networks is essential to the regulation of cell and tissue shape. Here, we examine Rab protein distributions during Drosophila epithelial tissue remodeling and show that Rab35 is dynamically planar polarized. Rab35 compartments are enriched at contractile interfaces of intercalating cells and provide the first evidence of interfacial monopolarity. When Rab35 function is disrupted, apical area oscillations still occur and contractile steps are observed. However, contractions are followed by reversals and interfaces fail to shorten, demonstrating that Rab35 functions as a ratchet ensuring unidirectional movement. Although actomyosin forces have been thought to drive interface contraction, initiation of Rab35 compartments does not require Myosin II function. However, Rab35 compartments do not terminate and continue to grow into large elongated structures following actomyosin disruption. Finally, Rab35 represents a common contractile cell-shaping mechanism, as mesoderm invagination fails in Rab35 compromised embryos and Rab35 localizes to constricting surfaces.Various stages of tissue morphogenesis involve the contraction of epithelial surfaces. Here, the authors identify the Rab GTPase Rab35 as an essential component of this contractile process, which functions as a membrane ratchet to ensure unidirectional movement of intercalating cells.

Indexed as

ActomyosinAnimalsAnimals, Genetically ModifiedCell CompartmentationCell MembraneCell PolarityCell ShapeDrosophila melanogasterDrosophila ProteinsEndosomesEpithelial CellsMyosin Type IIrab11 GTP-Binding Proteinsrab5 GTP-Binding Proteinsrab GTP-Binding ProteinsActomyosinDrosophila ProteinsMyosin Type IIrab11 GTP-Binding ProteinsRab11 protein, DrosophilaRab35 protein, Drosophilarab5 GTP-Binding ProteinsRab5 protein, Drosophilarab GTP-Binding Proteins

Identifiers

PMID28883443
PMCPMC5589913
OpenAlexW2751884145

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.