Evidence map›Paper›PMID 23699395›Full record

ArticleMolecular biology of the cell2013

SHIP2 regulates epithelial cell polarity through its lipid product, which binds to Dlg1, a pathway subverted by hepatitis C virus core protein.

Aline Awad, Sokhavuth Sar, Ronan Barré, Clotilde Cariven, Mickael Marin, Jean Pierre Salles, Christophe Erneux, Didier Samuel, Ama Gassama-Diagne

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

23 citing papers in PubMed, 45 citations in OpenAlex.

  1. Viral subversion of the cell polarity regulator Scribble.Biochemical Society transactions · 2023
    Review
  2. Article
  3. Review
  4. Review
  5. Membrane Lipids in Epithelial Polarity: Sorting out the PIPs.Frontiers in cell and developmental biology · 2022
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. PDZ Domains as Drug Targets.Advanced therapeutics · 2019
    Review
  13. Review
  14. The phospholipid PI(3,4)PNature communications · 2018
    Article
  15. Review
  16. INPPL1 gene mutations in opsismodysplasia.Journal of human genetics · 2017
    Review
  17. Review
  18. Article
  19. Review
  20. 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

9 authors at 3 institutions in 2 countries.

Aline AwadUniversité Paris-Sud, UMR-S 785, F-94800 Villejuif, France.
Sokhavuth Sar
Ronan Barré
Clotilde Cariven
Mickael Marin
Jean Pierre Salles
Christophe Erneux
Didier Samuel
Ama Gassama-Diagne
Université Paris-Sud · FRUniversité Toulouse III - Paul Sabatier · FRUniversité Libre de Bruxelles · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The main targets of hepatitis C virus (HCV) are hepatocytes, the highly polarized cells of the liver, and all the steps of its life cycle are tightly dependent on host lipid metabolism. The interplay between polarity and lipid metabolism in HCV infection has been poorly investigated. Signaling lipids, such as phosphoinositides (PIs), play a vital role in polarity, which depends on the distribution and expression of PI kinases and PI phosphatases. In this study, we report that HCV core protein, expressed in Huh7 and Madin-Darby canine kidney (MDCK) cells, disrupts apicobasal polarity. This is associated with decreased expression of the polarity protein Dlg1 and the PI phosphatase SHIP2, which converts phosphatidylinositol 3,4,5-trisphosphate into phosphatidylinositol 4,5-bisphosphate (PtdIns(3,4)P2). SHIP2 is mainly localized at the basolateral membrane of polarized MDCK cells. In addition, PtdIns(3,4)P2 is able to bind to Dlg1. SHIP2 small interfering RNA or its catalytically dead mutant disrupts apicobasal polarity, similar to HCV core. In core-expressing cells, RhoA activity is inhibited, whereas Rac1 is activated. Of interest, SHIP2 expression rescues polarity, RhoA activation, and restricted core level in MDCK cells. We conclude that SHIP2 is an important regulator of polarity, which is subverted by HCV in epithelial cells. It is suggested that SHIP2 could be a promising target for anti-HCV treatment.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCell LineCell PolarityDiscs Large Homolog 1 ProteinDogsEpithelial CellsGene Expression RegulationHepacivirusHepatocytesHost-Pathogen InteractionsHumansMembrane ProteinsPhosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesPhosphatidylinositol 3-KinasesPhosphatidylinositol 4,5-DiphosphateAdaptor Proteins, Signal TransducingDiscs Large Homolog 1 ProteinDLG1 protein, humanINPPL1 protein, humanMembrane Proteinsphosphatidylinositol 3,4,5-triphosphatePhosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesPhosphatidylinositol 3-Kinasesphosphatidylinositol-3-phosphatasePhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesProtein IsoformsRNA, Small InterferingViral Core Proteins

Identifiers

PMID23699395
PMCPMC3708724
OpenAlexW2109410151

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.