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      SHP-2 tyrosine phosphatase as an intracellular target of Helicobacter pylori CagA protein.

      Science (New York, N.Y.)

      src Homology Domains, Amino Acid Substitution, Virulence, Transfection, SH2 Domain-Containing Protein Tyrosine Phosphatases, metabolism, Recombinant Fusion Proteins, genetics, chemistry, antagonists & inhibitors, Protein Tyrosine Phosphatases, Protein Tyrosine Phosphatase, Non-Receptor Type 6, Protein Tyrosine Phosphatase, Non-Receptor Type 11, Phosphotyrosine, Phosphorylation, Phenotype, Mutation, Intracellular Signaling Peptides and Proteins, Humans, pathogenicity, Helicobacter pylori, enzymology, cytology, Gastric Mucosa, pharmacology, Enzyme Inhibitors, Dipeptides, Cell Size, Cell Membrane, COS Cells, Bacterial Proteins, Antigens, Bacterial, Animals

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          Abstract

          Helicobacter pylori CagA protein is associated with severe gastritis and gastric carcinoma. CagA is injected from the attached Helicobacter pylori into host cells and undergoes tyrosine phosphorylation. Wild-type but not phosphorylation-resistant CagA induced a growth factor-like response in gastric epithelial cells. Furthermore, CagA formed a physical complex with the SRC homology 2 domain (SH2)-containing tyrosine phosphatase SHP-2 in a phosphorylation-dependent manner and stimulated the phosphatase activity. Disruption of the CagA-SHP-2 complex abolished the CagA-dependent cellular response. Conversely, the CagA effect on cells was reproduced by constitutively active SHP-2. Thus, upon translocation, CagA perturbs cellular functions by deregulating SHP-2.

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          Journal
          10.1126/science.1067147
          11743164

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