Evidence map›Paper›PMID 29758044›Full record

ArticlePLoS genetics2018

Prickle is phosphorylated by Nemo and targeted for degradation to maintain Prickle/Spiny-legs isoform balance during planar cell polarity establishment.

Giovanna M Collu, Andreas Jenny, Konstantin Gaengel, Ivana Mirkovic, Mei-Ling Chin, Ursula Weber, Michael J Smith, Marek Mlodzik

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.3field-weighted citation impact, top 43% 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

8 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Wallenda-Nmo Axis Regulates Growth via Hippo Signaling.Frontiers in cell and developmental biology · 2021
    Article
  7. Article
  8. Review
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

8 authors at 1 institution in 1 country.

Giovanna M ColluDepartment of Cell, Developmental & Regenerative Biology and Graduate School of Biomedical Sciences, Icahn School of Medicine at Mount Sinai, New York, New York, United States of America.
Andreas JennyDepartment of Cell, Developmental & Regenerative Biology and Graduate School of Biomedical Sciences, Icahn School of Medicine at Mount Sinai, New York, New York, United States of America.
Konstantin GaengelDepartment of Cell, Developmental & Regenerative Biology and Graduate School of Biomedical Sciences, Icahn School of Medicine at Mount Sinai, New York, New York, United States of America.
Ivana MirkovicDepartment of Cell, Developmental & Regenerative Biology and Graduate School of Biomedical Sciences, Icahn School of Medicine at Mount Sinai, New York, New York, United States of America.
Mei-Ling ChinDepartment of Cell, Developmental & Regenerative Biology and Graduate School of Biomedical Sciences, Icahn School of Medicine at Mount Sinai, New York, New York, United States of America.
Ursula WeberDepartment of Cell, Developmental & Regenerative Biology and Graduate School of Biomedical Sciences, Icahn School of Medicine at Mount Sinai, New York, New York, United States of America.
Michael J SmithDepartment of Cell, Developmental & Regenerative Biology and Graduate School of Biomedical Sciences, Icahn School of Medicine at Mount Sinai, New York, New York, United States of America.
Marek MlodzikDepartment of Cell, Developmental & Regenerative Biology and Graduate School of Biomedical Sciences, Icahn School of Medicine at Mount Sinai, New York, New York, United States of America.ORCID 0000-0002-0628-3465
Icahn School of Medicine at Mount Sinai · US

Funding

THE TISCH CANCER INSTITUTE - CANCER CENTER SUPPORT GRANTP30CA196521 · NCI · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI Deanna L Benson · 2015 to 2026
$35.4M
Retinal Patterning During Eye DevelopmentR01EY013256 · NEI · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI Marek Mlodzik · 2001 to 2026
$10.0M
Wnt/Frizzled-PCP signaling in development and diseaseR35GM127103 · NIGMS · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI Marek Mlodzik · 2018 to 2026
$5.6M
Planar Cell Polarity regulation by transmembrane proteinsR01GM102811 · NIGMS · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI MLODZIK, MAREK · 2012 to 2017
$2.1M
WNK KINASES IN DEVELOPMENTR01GM115646 · NIGMS · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI JENNY, ANDREAS · 2016 to 2019
$1.5M
NCI NIH HHS P30 CA196521NEI NIH HHS R01 EY013256NIGMS NIH HHS R01 GM102811NIGMS NIH HHS R01 GM115646NIGMS NIH HHS R35 GM127103NIH HHS EY013256NIH HHS GM115646NIH HHS GM127103
6 · The paper itself

Abstract

Planar cell polarity (PCP) instructs tissue patterning in a wide range of organisms from fruit flies to humans. PCP signaling coordinates cell behavior across tissues and is integrated by cells to couple cell fate identity with position in a developing tissue. In the fly eye, PCP signaling is required for the specification of R3 and R4 photoreceptors based upon their positioning relative to the dorso-ventral axis. The 'core' PCP pathway involves the asymmetric localization of two distinct membrane-bound complexes, one containing Frizzled (Fz, required in R3) and the other Van Gogh (Vang, required in R4). Inhibitory interactions between the cytosolic components of each complex reinforce asymmetric localization. Prickle (Pk) and Spiny-legs (Pk-Sple) are two antagonistic isoforms of the prickle (pk) gene and are cytoplasmic components of the Vang complex. The balance between their levels is critical for tissue patterning, with Pk-Sple being the major functional isoform in the eye. Here we uncover a post-translational role for Nemo kinase in limiting the amount of the minor isoform Pk. We identified Pk as a Nemo substrate in a genome-wide in vitro band-shift screen. In vivo, nemo genetically interacts with pkpk but not pksple and enhances PCP defects in the eye and leg. Nemo phosphorylation limits Pk levels and is required specifically in the R4 photoreceptor like the major isoform, Pk-Sple. Genetic interaction and biochemical data suggest that Nemo phosphorylation of Pk leads to its proteasomal degradation via the Cullin1/SkpA/Slmb complex. dTAK and Homeodomain interacting protein kinase (Hipk) may also act together with Nemo to target Pk for degradation, consistent with similar observations in mammalian studies. Our results therefore demonstrate a mechanism to maintain low levels of the minor Pk isoform, allowing PCP complexes to form correctly and specify cell fate.

Indexed as

AnimalsAnimals, Genetically ModifiedCell LineCell PolarityDNA-Binding ProteinsDrosophila melanogasterDrosophila ProteinsEyeFrizzled ReceptorsLIM Domain ProteinsMembrane ProteinsMitogen-Activated Protein KinasesPhosphorylationProtein IsoformsProteolysisSignal TransductionDNA-Binding ProteinsDrosophila ProteinsFrizzled ReceptorsLIM Domain ProteinsMembrane ProteinsMitogen-Activated Protein Kinasesnmo protein, Drosophilapk protein, DrosophilaProtein IsoformsVang protein, Drosophila

Identifiers

PMID29758044
PMCPMC5967807
OpenAlexW2802747845

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.