The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
c‐Src/Lyn kinases activate Helicobacter pylori CagA through tyrosine phosphorylation of the EPIYA motifs
Abstract
Summary: The human pathogen Helicobacter pylori colonizes the mucous layer of the stomach. During parasitic infection, freely swimming bacteria adhere to the gastric epithelial cells and trigger intracellular signalling pathways. This process requires the translocation of the effector protein CagA into the host cell through a specialized type IV secretion system encoded in the cag pathogenicity island. Following transfer, CagA is phosphorylated on tyrosine re‐sidues by a host cell kinase. Here, we describe how the tyrosine phosphorylation of CagA is restricted to a previously identified repeated sequence called D1. This sequence is located in the C‐terminal half of the protein and contains the five‐amino‐acid motif EPIYA, which is amplified by duplications in a large fraction of clinical isolates. Tyrosine phosphorylation of CagA is essential for the activation process that leads to dramatic changes in the morphology of cells growing in culture. In addition, we observed that two members of the src kinases family, c‐Src and Lyn, account for most of the CagA‐specific kinase activity in host cell lysates. Thus, CagA translocation followed by tyrosine phosphorylation at the EPIYA motifs promotes a growth factor‐like response with intense cytoskeletal rearrangements, cell elongation effects and increased cellular motility.
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Translocation of Helicobacter pylori CagA into Gastric Epithelial Cells by Type IV Secretion
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Self-citationEnteropathogenic E. coli (EPEC) Transfers Its Receptor for Intimate Adherence into Mammalian Cells
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Self-citationAutophosphorylation of the Focal Adhesion Kinase, ppl25FAK, Directs SH2-Dependent Binding of pp60src
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Cited by
Pathogenesis of Helicobacter pylori Infection
Kusters, J. G., van Vliet, A. H. M., & Kuipers, E. J. (2006) · Clinical Microbiology Reviews · doi:10.1128/cmr.00054-05 · Cited by 2,526
Helicobacter pylori and Gastric Cancer: Factors That Modulate Disease Risk
Wroblewski, L. E., Peek, R. M., & Wilson, K. T. (2010) · Clinical Microbiology Reviews · doi:10.1128/cmr.00011-10 · Cited by 1,442
Helicobacter pylori: gastric cancer and beyond
Polk, D. B., & Peek, R. M. (2010) · Nature Reviews Cancer · doi:10.1038/nrc2857 · Cited by 1,158
Mechanisms of disease: Helicobacter pylori virulence factors
Yamaoka, Y. (2010) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2010.154 · Cited by 666
Host-Bacterial Interactions in Helicobacter pylori Infection
Amieva, M. R., & El–Omar, E. M. (2008) · Gastroenterology · doi:10.1053/j.gastro.2007.11.009 · Cited by 632
Metadata
- Authors
- Stein, M., Bagnoli, F., Halenbeck, R., Rappuoli, R., Fantl, W. J., & Covacci, A.
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2002-02
- Volume
- 43
- Issue
- 4
- Pages
- 971-980
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W2116757244
- Cited by
- 437
- References
- 32
- FWCI
- 26.32
- Type
- journal article
- Language
- en
- Open access
- closed
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- Stein, M., Bagnoli, F., Halenbeck, R., Rappuoli, R., Fantl, W. J., & Covacci, A. (2002). c‐Src/Lyn kinases activate Helicobacter pylori CagA through tyrosine phosphorylation of the EPIYA motifs. Molecular Microbiology. https://doi.org/10.1046/j.1365-2958.2002.02781.x
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