ArticleCellular microbiology2015
CagA of Helicobacter pylori interacts with and inhibits the serine-threonine kinase PRK2.
Article in Cellular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Microbial oncogenesis within the gastric niche: how the gastric microbiota influencesFrontiers in microbiology · 2025Review
- T4SEpp: A pipeline integrating protein language models to predict bacterial type IV secreted effectors.Computational and structural biotechnology journal · 2024Article
- Role of MARK2 in the nervous system and cancer.Cancer gene therapy · 2024Review
- The structure and function of protein kinase C-related kinases (PRKs).Biochemical Society transactions · 2021Review
- Inhibition of polarity-regulating kinase PAR1b contributes to Helicobacter pylori inflicted DNA Double Strand Breaks in gastric cells.Cell cycle (Georgetown, Tex.) · 2019Article
- Microtubule affinity-regulating kinases are potential druggable targets for Alzheimer's disease.Cellular and molecular life sciences : CMLS · 2017Review
- EPEC effector EspF promotes Crumbs3 endocytosis and disrupts epithelial cell polarity.Cellular microbiology · 2017Article
- Modulation of epithelial cell polarity by bacterial pathogens.Annals of the New York Academy of Sciences · 2017Review
- Microbial carcinogenic toxins and dietary anti-cancer protectants.Cellular and molecular life sciences : CMLS · 2017Review
- Targeting the Mucosal Barrier: How Pathogens Modulate the Cellular Polarity Network.Cold Spring Harbor perspectives in biology · 2017Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
CagA is a multifunctional toxin of Helicobacter pylori that is secreted into host epithelial cells by a type IV secretion system. Following host cell translocation, CagA interferes with various host-cell signalling pathways. Most notably this toxin is involved in the disruption of apical-basolateral cell polarity and cell adhesion, as well as in the induction of cell proliferation, migration and cell morphological changes. These are processes that also play an important role in epithelial-to-mesenchymal transition and cancer cell invasion. In fact, CagA is considered as the only known bacterial oncoprotein. The cellular effects are triggered by a variety of CagA activities including the inhibition of serine-threonine kinase Par1b/MARK2 and the activation of tyrosine phosphatase SHP-2. Additionally, CagA was described to affect the activity of Src family kinases and C-terminal Src kinase (Csk) suggesting that interference with multiple cellular kinase- and phosphatase-associated signalling pathways is a major function of CagA. Here, we describe the effect of CagA on protein kinase C-related kinase 2 (PRK2), which acts downstream of Rho GTPases and is known to affect cytoskeletal rearrangements and cell polarity. CagA interacts with PRK2 and inhibits its kinase activity. Because PRK2 has been linked to cytoskeletal rearrangements and establishment of cell polarity, we suggest that CagA may hijack PRK2 to further manipulate cancer-related signalling pathways.
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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 OpenQuestion graph.