Evidence map›Paper›PMID 21044957›Full record

ArticleThe Journal of biological chemistry2010

Identification of transmembrane protein 88 (TMEM88) as a dishevelled-binding protein.

Ho-Jin Lee, David Finkelstein, Xiaofeng Li, Dianqing Wu, De-Li Shi, Jie J Zheng

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 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

34 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. PDZ Domains as Drug Targets.Advanced therapeutics · 2019
    Review
  12. Article
  13. Review
  14. TMEM Proteins in Cancer: A Review.Frontiers in pharmacology · 2018
    Review
  15. Article
  16. Article
  17. Modulating the wnt signaling pathway with small molecules.Protein science : a publication of the Protein Society · 2017
    Review
  18. Article
  19. Article
  20. Article
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

6 authors at 3 institutions in 2 countries.

Ho-Jin LeeDepartment of Structural Biology, St Jude Children’s Research Hospital, Memphis, Tennessee 38105, USA.
David Finkelstein
Xiaofeng Li
Dianqing Wu
De-Li Shi
Jie J Zheng
St. Jude Children's Research Hospital · USYale University · USLaboratoire de Biologie du Développement · FR

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
Wnt signalingR01CA139395 · NCI · YALE UNIVERSITY · PI WU, DIANQING · 2009 to 2013
$1.9M
Therapeutic Targeting of Wnt SignalingR01CA132317 · NCI · YALE UNIVERSITY · PI WU, DIANQING · 2008 to 2012
$1.7M
Mechanisms of Different Wnt SignalsR01GM081492 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI ZHENG, JIE J. · 2007 to 2010
$1.2M
NCI NIH HHS CA21765NCI NIH HHS P30 CA021765NCI NIH HHS R01 CA132317NCI NIH HHS R01 CA139395NIGMS NIH HHS GM081492NIGMS NIH HHS R01 GM081492
6 · The paper itself

Abstract

Wnt signaling pathways are involved in embryonic development and adult tissue maintenance and have been implicated in tumorigenesis. Dishevelled (Dvl/Dsh) protein is one of key components in Wnt signaling and plays essential roles in regulating these pathways through protein-protein interactions. Identifying and characterizing Dvl-binding proteins are key steps toward understanding biological functions. Given that the tripeptide VWV (Val-Trp-Val) binds to the PDZ domain of Dvl, we searched publically available databases to identify proteins containing the VWV motif at the C terminus that could be novel Dvl-binding partners. On the basis of the cellular localization and expression patterns of the candidates, we selected for further study the TMEM88 (target protein transmembrane 88), a two-transmembrane-type protein. The interaction between the PDZ domain of Dvl and the C-terminal tail of TMEM88 was confirmed by using NMR and fluorescence spectroscopy. Furthermore, in HEK293 cells, TMEM88 attenuated the Wnt/β-catenin signaling induced by Wnt-1 ligand in a dose-dependent manner, and TMEM88 knockdown by RNAi increased Wnt activity. In Xenopus, TMEM88 protein is sublocalized at the cell membrane and inhibits Wnt signaling induced by Xdsh but not β-catenin. In addition, TMEM88 protein inhibits the formation of a secondary axis normally induced by Xdsh. The findings suggest that TMEM88 plays a role in regulating Wnt signaling. Indeed, analysis of microarray data revealed that the expression of the Tmem88 gene was strongly correlated with that of Wnt signaling-related genes in embryonic mouse intestines. Together, we propose that TMEM88 associates with Dvl proteins and regulates Wnt signaling in a context-dependent manner.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid MotifsAmino Acid SequenceAnimalsDishevelled ProteinsHumansLigandsMagnetic Resonance SpectroscopyMembrane ProteinsMiceMolecular Sequence DataPhosphoproteinsProtein BindingProtein Interaction MappingSequence Homology, Amino AcidSignal TransductionAdaptor Proteins, Signal TransducingDishevelled ProteinsDVL1 protein, XenopusLigandsMembrane ProteinsPhosphoproteinsTMEM88 protein, humanTMEM88 protein, mouseWnt1 ProteinWNT1 protein, humanWnt1 protein, mouseXenopus Proteins

Identifiers

PMID21044957
PMCPMC3009882
OpenAlexW2059410615

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.