Evidence map›Paper›PMID 20177058›Full record

ArticleThe Journal of biological chemistry2010

Myristoylated Naked2 antagonizes Wnt-beta-catenin activity by degrading Dishevelled-1 at the plasma membrane.

Tianhui Hu, Cunxi Li, Zheng Cao, Terence J Van Raay, Jason G Smith, Karl Willert, Lila Solnica-Krezel, Robert J Coffey

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. 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
2.3field-weighted citation impact, top 12% 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

41 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
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  7. Metabolic transitions regulate global protein fatty acylation.The Journal of biological chemistry · 2024
    Article
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  10. Article
  11. Article
  12. Review
  13. Article
  14. 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

8 authors at 2 institutions in 2 countries.

Tianhui HuCancer Research Center, Xiamen University Medical College, Xiamen, 361005 Fujian, China.
Cunxi Li
Zheng Cao
Terence J Van Raay
Jason G Smith
Karl Willert
Lila Solnica-Krezel
Robert J Coffey
Vanderbilt University · USUniversity of California, San Diego · US

Funding

Understanding and Controlling p120 Dysfunction in CRCP50CA095103 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI COFFEY, ROBERT J. · 2002 to 2017
$33.6M
TRANSFORMING GROWTH FACTORS IN COLONIC NEOPLASIAR01CA046413 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI COFFEY, ROBERT J. · 1988 to 2016
$8.8M
Prevention &Metastasis: Final Frontiers in Colon CancerU01CA084239 · NCI · VANDERBILT UNIVERSITY · PI COFFEY, ROBERT J. · 1999 to 2009
$8.0M
TRAINING GRANT IN MECHANISMS OF VASCULAR DISEASET32HL007751 · NHLBI · VANDERBILT UNIVERSITY · PI BOCK, PAUL E · 1994 to 2014
$6.6M
GENETIC ANALYSIS OF CONVERGENT EXTENSION IN ZEBRAFISHR01GM055101 · NIGMS · WASHINGTON UNIVERSITY · PI SOLNICAKREZEL, LILIANNA · 1997 to 2014
$4.5M
NCI NIH HHS 5P50CA095103NCI NIH HHS 5R01CA046413NCI NIH HHS P50 CA095103NCI NIH HHS R01 CA046413NCI NIH HHS U01 CA084239NHLBI NIH HHS 5T32HL007751NHLBI NIH HHS T32 HL007751NIGMS NIH HHS R01 GM055101NIGMS NIH HHS R01 GM55101
6 · The paper itself

Abstract

In Drosophila, naked cuticle is an inducible antagonist of the Wnt-beta-catenin pathway, likely acting at the level of Dishevelled (Dsh/Dvl), an essential component of this pathway. The mechanism by which naked cuticle and its two vertebrate orthologs, Naked1 (NKD1) and Naked2 (NKD2), inhibit Dvl function is unknown. NKD2 is myristoylated, a co-translational modification that leads to its plasma membrane localization. In contrast, myristoylation-deficient G2A NKD2 is cytoplasmic. Herein we show that the ability of Nkd2/NKD2 to antagonize Wnt-beta-catenin activity during zebrafish embryonic development and in mammalian HEK293 cells is myristoylation-dependent. NKD2 and Dvl-1 interact and co-localize at the lateral membrane of polarized epithelial cells. In reciprocal overexpression and siRNA knockdown experiments, NKD2 and Dvl-1 destabilize each other via enhanced polyubiquitylation; this effect is also dependent upon Naked2 myristoylation. Cell fractionation and ubiquitylation assays indicate that endogenous NKD2 interacts with a slower migrating, ubiquitylated form of Dvl-1 in plasma membrane fractions. These results provide a mechanism by which NKD2 antagonizes Wnt signaling: myristoylated NKD2 interacts with Dvl-1 at the plasma membrane, and this interaction leads to their mutual ubiquitin-mediated proteasomal degradation.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsbeta CateninCaco-2 CellsCalcium-Binding ProteinsCarrier ProteinsCell MembraneCell PolarityDishevelled ProteinsDogsDrosophilaDrosophila ProteinsEpithelial CellsHumansMyristic AcidPhosphoproteinsAdaptor Proteins, Signal Transducingbeta CateninCalcium-Binding ProteinsCarrier ProteinsDishevelled ProteinsDrosophila Proteinsdsh protein, DrosophilaDVL1 protein, humanMyristic AcidNKD1 protein, humanNKD2 protein, humanPhosphoproteinsProteasome Endopeptidase ComplexWnt Proteins

Identifiers

PMID20177058
PMCPMC2859517
OpenAlexW2018866580

What OpenQuestion holds

Textmetadata
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.