Structure and function of Helicobacter pylori CagA, the first-identified bacterial protein involved in human cancer
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- HATAKEYAMA Masanori
- Department of Microbiology, Graduate School of Medicine, The University of Tokyo
書誌事項
- タイトル別名
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- Structure and function of <i>Helicobacter pylori</i> CagA, the first-identified bacterial protein involved in human cancer
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<p>Chronic infection with Helicobacter pylori cagA-positive strains is the strongest risk factor of gastric cancer. The cagA gene-encoded CagA protein is delivered into gastric epithelial cells via bacterial type IV secretion, where it undergoes tyrosine phosphorylation at the Glu-Pro-Ile-Tyr-Ala (EPIYA) motifs. Delivered CagA then acts as a non-physiological scaffold/hub protein by interacting with multiple host signaling molecules, most notably the pro-oncogenic phosphatase SHP2 and the polarity-regulating kinase PAR1/MARK, in both tyrosine phosphorylation-dependent and -independent manners. CagA-mediated manipulation of intracellular signaling promotes neoplastic transformation of gastric epithelial cells. Transgenic expression of CagA in experimental animals has confirmed the oncogenic potential of the bacterial protein. Structural polymorphism of CagA influences its scaffold function, which may underlie the geographic difference in the incidence of gastric cancer. Since CagA is no longer required for the maintenance of established gastric cancer cells, studying the role of CagA during neoplastic transformation will provide an excellent opportunity to understand molecular processes underlying “Hit-and-Run” carcinogenesis.</p>
収録刊行物
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- Proceedings of the Japan Academy. Ser. B: Physical and Biological Sciences
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Proceedings of the Japan Academy. Ser. B: Physical and Biological Sciences 93 (4), 196-219, 2017
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詳細情報 詳細情報について
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- CRID
- 1390282679122571648
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- NII論文ID
- 130006770746
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- NII書誌ID
- AA00785485
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- ISSN
- 13492896
- 03862208
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- NDL書誌ID
- 028139012
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- PubMed
- 28413197
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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