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• W2079130007 abstract "CagA, a major virulence factor of Helicobacter pylori (Hp), is delivered into gastric epithelial cells and exists in phosphorylated and nonphosphorylated forms. The biological activity of the phosphorylated form is well established; however, function(s) of the nonphosphorylated form remain elusive. Here, we report that a conserved motif in the C-terminal region of CagA, which is distinct from the EPIYA motifs used for phosphorylation and which we designate CRPIA (conserved repeat responsible for phosphorylation-independent activity), plays pivotal roles in Hp pathogenesis. The CRPIA motif in nonphosphorylated CagA was involved in interacting with activated Met, the hepatocyte growth factor receptor, leading to the sustained activation of phosphatidylinositol 3-kinase/Akt signaling in response to Hp infection. This in turn led to the activation of β-catenin and NF-κB signaling, which promote proliferation and inflammation, respectively. Thus, nonphosphorylated CagA activity contributes to the epithelial proliferative and proinflammatory responses associated with development of chronic gastritis and gastric cancer." @default.
• W2079130007 created "2016-06-24" @default.
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• W2079130007 date "2009-01-01" @default.
• W2079130007 modified "2023-10-11" @default.
• W2079130007 title "Helicobacter pylori CagA Phosphorylation-Independent Function in Epithelial Proliferation and Inflammation" @default.
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• W2079130007 doi "https://doi.org/10.1016/j.chom.2008.11.010" @default.
• W2079130007 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19154985" @default.
• W2079130007 hasPublicationYear "2009" @default.
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