ArticleCancer science2020
Helicobacter pylori CagA oncoprotein interacts with SHIP2 to increase its delivery into gastric epithelial cells.
Article in Cancer science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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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.
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Who cites it
20 citing papers in PubMed, 25 citations in OpenAlex.
- CagA promotes gastric cancer stemness and metastasis via DNMT1-mediated epigenetic silencing of BEX1.Cancer gene therapy · 2026Article
- Histomorphological analysis of the relationship between Helicobacter pylori infection of the gastric mucosa and host immunity strength.Journal of molecular histology · 2026Article
- Mitochondrial Stress inAntioxidants (Basel, Switzerland) · 2026Review
- Pathogenicity ofWorld journal of clinical oncology · 2025Review
- Garvicin Q-producing Lactococcus garvieae LG3092: its role in mitigating dysbiosis and H. pylori-associated gastritis.NPJ biofilms and microbiomes · 2025Article
- Helicobacter pylori and gastric cancer: mechanisms and new perspectives.Journal of hematology & oncology · 2025Review
- Article
- Amino acid deletions at positions 893 and 894 of cytotoxin-associated gene A protein affectWorld journal of gastroenterology · 2024Article
- The Functional Roles of the Src Homology 2 Domain-Containing Inositol 5-Phosphatases SHIP1 and SHIP2 in the Pathogenesis of Human Diseases.International journal of molecular sciences · 2024Review
- Helicobacter pylori CagA promotes immune evasion of gastric cancer by upregulating PD-L1 level in exosomes.iScience · 2023Article
- Reactive Oxygen Species andAntioxidants (Basel, Switzerland) · 2023Review
- Review
- Establishment and Methodological Evaluation of a Method for Rapid Detection ofInfection and drug resistance · 2023Article
- Influence ofWorld journal of clinical oncology · 2022Review
- Structural Insights into the Binding Propensity of Human SHIP2 SH2 to Oncogenic CagA Isoforms fromInternational journal of molecular sciences · 2022Article
- Positive Selection of Mutations in the Helicobacter pyloriInfection and immunity · 2022Article
- Mouse Gastric Epithelial Cells Resist CagA Delivery by theInternational journal of molecular sciences · 2022Article
- Critical roles of PTPN family members regulated by non-coding RNAs in tumorigenesis and immunotherapy.Frontiers in oncology · 2022Review
- Review
- Helicobacter pylori CagA oncoprotein interacts with SHIP2 to increase its delivery into gastric epithelial cells.Cancer science · 2020Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
Abstract
Chronic infection with Helicobacter pylori cagA-positive strains is causally associated with the development of gastric diseases, most notably gastric cancer. The cagA-encoded CagA protein, which is injected into gastric epithelial cells by bacterial type IV secretion, undergoes tyrosine phosphorylation at the Glu-Pro-Ile-Tyr-Ala (EPIYA) segments (EPIYA-A, EPIYA-B, EPIYA-C, and EPIYA-D), which are present in various numbers and combinations in its C-terminal polymorphic region, thereby enabling CagA to promiscuously interact with SH2 domain-containing host cell proteins, including the prooncogenic SH2 domain-containing protein tyrosine phosphatase 2 (SHP2). Perturbation of host protein functions by aberrant complex formation with CagA has been considered to contribute to the development of gastric cancer. Here we show that SHIP2, an SH2 domain-containing phosphatidylinositol 5'-phosphatase, is a hitherto undiscovered CagA-binding host protein. Similar to SHP2, SHIP2 binds to the Western CagA-specific EPIYA-C segment or East Asian CagA-specific EPIYA-D segment through the SH2 domain in a tyrosine phosphorylation-dependent manner. In contrast to the case of SHP2, however, SHIP2 binds more strongly to EPIYA-C than to EPIYA-D. Interaction with CagA tethers SHIP2 to the plasma membrane, where it mediates production of phosphatidylinositol 3,4-diphosphate [PI(3,4)P
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Registered trials
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 Socratic graph.