Evidence map›Paper›PMID 27445265›Full record

ArticleScientific reports2016

Impact of structural polymorphism for the Helicobacter pylori CagA oncoprotein on binding to polarity-regulating kinase PAR1b.

Hiroko Nishikawa, Takeru Hayashi, Fumio Arisaka, Toshiya Senda, Masanori Hatakeyama

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

15 citing papers in PubMed, 27 citations in OpenAlex.

  1. Microbiology and molecular biology reviews : MMBR · 2026
    Review
  2. Mitochondrial Stress inAntioxidants (Basel, Switzerland) · 2026
    Review
  3. Review
  4. Article
  5. Interesting Biochemistries in the Structure and Function of Bacterial Effectors.Frontiers in cellular and infection microbiology · 2021
    Review
  6. Article
  7. Cytotoxin-associated gene-A-seropositivity andInternational journal of cardiology. Heart & vasculature · 2020
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Regulation of Cell Polarity by PAR-1/MARK Kinase.Current topics in developmental biology · 2017
    Review
  14. Petri Net-Based Model ofFrontiers in microbiology · 2017
    Article
  15. Structure and function of Helicobacter pylori CagA, the first-identified bacterial protein involved in human cancer.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2017
    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

5 authors at 4 institutions in 1 country.

Hiroko NishikawaDivision of Microbiology, Graduate School of Medicine, The University of Tokyo, Tokyo 113-0033, Japan.
Takeru HayashiDivision of Microbiology, Graduate School of Medicine, The University of Tokyo, Tokyo 113-0033, Japan.
Fumio ArisakaCollege of Bioresource Sciences, Nihon University, Fujisawa 252-0880, Japan.
Toshiya SendaCREST, Japan Science and Technology Agency, Saitama 332-0012, Japan.
Masanori HatakeyamaDivision of Microbiology, Graduate School of Medicine, The University of Tokyo, Tokyo 113-0033, Japan.
The University of Tokyo · JPHigh Energy Accelerator Research Organization · JPJapan Science and Technology Agency · JPNihon University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chronic infection with cagA-positive Helicobacter pylori is the strongest risk factor for atrophic gastritis, peptic ulcers, and gastric cancer. CagA, the product of the cagA gene, is a bacterial oncoprotein, which, upon delivery into gastric epithelial cells, binds to and inhibits the polarity-regulating kinase, partitioning-defective 1b (PAR1b) [also known as microtubule affinity-regulating kinase 2 (MARK2)], via its CagA multimerization (CM) motif. The inhibition of PAR1b elicits junctional and polarity defects, rendering cells susceptible to oncogenesis. Notably, the polymorphism in the CM motif has been identified among geographic variants of CagA, differing in either the copy number or the sequence composition. In this study, through quantitative analysis of the complex formation between CagA and PAR1b, we found that several CagA species have acquired elevated PAR1b-binding activity via duplication of the CM motifs, while others have lost their PAR1b-binding activity. We also found that strength of CagA-PAR1b interaction was proportional to the degrees of stress fiber formation and tight junctional disruption by CagA in gastric epithelial cells. These results indicate that the CM polymorphism is a determinant for the magnitude of CagA-mediated deregulation of the cytoskeletal system and thereby possibly affects disease outcome of cagA-positive H. pylori infection, including gastric cancer.

Indexed as

Genetic VariationAmino Acid MotifsAntigens, BacterialBacterial ProteinsHelicobacter pyloriOncogene ProteinsProtein BindingProtein MultimerizationProtein Serine-Threonine KinasesAntigens, BacterialBacterial ProteinscagA protein, Helicobacter pyloriMARK2 protein, humanOncogene ProteinsProtein Serine-Threonine Kinases

Identifiers

PMID27445265
PMCPMC4957108
OpenAlexW2501758929

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.