Evidence map›Paper›PMID 21552260›Full record

ArticleNature structural & molecular biology2011

Nemo kinase phosphorylates β-catenin to promote ommatidial rotation and connects core PCP factors to E-cadherin-β-catenin.

Ivana Mirkovic, William J Gault, Maryam Rahnama, Andreas Jenny, Konstantin Gaengel, Darrell Bessette, Cara J Gottardi, Esther M Verheyen, Marek Mlodzik

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 41 citations in OpenAlex.

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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

9 authors at 4 institutions in 3 countries.

Ivana MirkovicDepartment of Developmental & Regenerative Biology, Mount Sinai School of Medicine, New York, New York, USA.
William J Gault
Maryam Rahnama
Andreas Jenny
Konstantin Gaengel
Darrell Bessette
Cara J Gottardi
Esther M Verheyen
Marek Mlodzik
Icahn School of Medicine at Mount Sinai · USSimon Fraser University · CAAlbert Einstein College of Medicine · USNorthwestern University · US

Funding

Establishment of Epithelial Planar Cell PolarityR01GM062917 · NIGMS · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI MLODZIK, MAREK · 2001 to 2013
$4.6M
Ommatidial rotation and cell motility in the eyeR01EY014597 · NEI · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI MLODZIK, MAREK · 2003 to 2011
$3.4M
Mechanism of nuclear signaling and cell-cell adhesion by cateninsR01GM076561 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI GOTTARDI, CARA J · 2006 to 2015
$2.8M
Planar Cell Polarity regulation by transmembrane proteinsR01GM102811 · NIGMS · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI MLODZIK, MAREK · 2012 to 2017
$2.1M
CIHR MOP 62895NEI NIH HHS R01 EY014597NEI NIH HHS R01 EY14597NIGMS NIH HHS GM076561NIGMS NIH HHS R01 GM062917NIGMS NIH HHS R01 GM076561NIGMS NIH HHS R01 GM102811
6 · The paper itself

Abstract

Frizzled planar cell polarity (PCP) signaling regulates cell motility in several tissues, including ommatidial rotation in Drosophila melanogaster. The Nemo kinase (Nlk in vertebrates) has also been linked to cell-motility regulation and ommatidial rotation but its mechanistic role(s) during rotation remain obscure. We show that nemo functions throughout the entire rotation movement, increasing the rotation rate. Genetic and molecular studies indicate that Nemo binds both the core PCP factor complex of Strabismus-Prickle, as well as the E-cadherin-β-catenin (E-cadherin-Armadillo in Drosophila) complex. These two complexes colocalize and, like Nemo, also promote rotation. Strabismus (also called Vang) binds and stabilizes Nemo asymmetrically within the ommatidial precluster; Nemo and β-catenin then act synergistically to promote rotation, which is mediated in vivo by Nemo's phosphorylation of β-catenin. Our data suggest that Nemo serves as a conserved molecular link between core PCP factors and E-cadherin-β-catenin complexes, promoting cell motility.

Indexed as

Cell MovementAnimalsbeta CateninCadherinsDNA-Binding ProteinsDrosophila melanogasterDrosophila ProteinsLIM Domain ProteinsMembrane ProteinsMitogen-Activated Protein KinasesOcular Physiological PhenomenaPhosphorylationProtein Bindingbeta CateninCadherinsDNA-Binding ProteinsDrosophila ProteinsLIM Domain ProteinsMembrane ProteinsMitogen-Activated Protein Kinasesnmo protein, Drosophilapk protein, Drosophilashg protein, DrosophilaVang protein, Drosophila

Identifiers

PMID21552260
PMCPMC3109122
OpenAlexW1975979806

What OpenQuestion holds

Textmetadata
LicenceTDM
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.