SHP-2 Tyrosine Phosphatase as an Intracellular Target of Helicobacter pylori CagA Protein

By H. Higashi, Ryouhei Tsutsumi, S. Muto, T. Sugiyama, T. Azuma, M. Asaka, Masanori Hatakeyama. Science, 2001

1,061 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology, Surgery

View Paper: https://www.semanticscholar.org/paper/d709099670d80b16a8bc6b2b16dbf6e9c22fbaef

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Immunology

1. Y. Yamaoka
2. R. Peek
3. Keith T. Wilson
4. Lydia E. Wroblewski
5. Masanori Hatakeyama

In Molecular Biology

1. P. Christie
2. Anica M Wandler
3. É. Cascales
4. Crystal M. Botham
5. K. Guillemin

In Surgery

1. Y. Yamaoka
2. R. Peek
3. Keith T. Wilson
4. Lydia E. Wroblewski
5. Masanori Hatakeyama

Citations in the corpus

• Transgenic expression of Helicobacter pylori CagA induces gastrointestinal and hematopoietic neoplasms in mouse (2008, background): “Tyrosine-phosphorylated CagA then specifically binds to and aberrantly activates SHP-2 tyrosine phosphatase (9, 14), a bona fide oncoprotein whose gain-of-function mutations are associated with human malignancies (13).”
• Pathogenicity Islands in Bacterial Pathogenesis (2004, background): “Type I strains carry genes encoding both, the cytotoxins CagA and VacA, while type II strains contain vacA genes only (376).”
• Helicobacter pylori and Gastric Cancer: Factors That Modulate Disease Risk (2010, background): “Phospho-CagA activates a eukaryotic tyrosine phosphatase (SHP-2), leading to sustained activation of extracellular signal-regulated kinases 1 and 2 (ERK1/2), Crk adaptor (133), and C-terminal Src kinase, in a tyrosine phosphorylation-dependent manner in which East Asian A-B-Dtype CagA exhibits stron”
• Oncogenic mechanisms of the Helicobacter pylori CagA protein (2004, background): “Tyrosine phosphorylation of CagA occurs at the EPIYA motif — a 5-amino-acid sequence (Glu-Pro-Ile-Tyr-Alu) that is present in the carboxy-terminal variable region of the protei”
• A Transgenic Drosophila Model Demonstrates That the Helicobacter pylori CagA Protein Functions as a Eukaryotic Gab Adaptor (2008, background): “Although CagA shares no sequence similarity with Gab proteins, CagA has been shown to activate SHP-2 in tissue culture cells, resulting in cell elongation [8,9].”
• Mechanisms of disease: Helicobacter pylori virulence factors (2010, background): “The best studied of the host signaling factors that interact with phosphorylated CagA is the Src homology-2 domain-containing phosphatase 2 (SHP2)”
• The versatile bacterial type IV secretion systems (2003, background): “A CagA interaction with the tyrosine phosphatase SHP2 stimulates SHP2 phosphatase activity, which, in turn, might be responsible for the observed dephosphorylation of several cellular protein”
• Helicobacter pylori: gastric cancer and beyond (2010, background): “Intracellular phospho-CagA activates a cellular phosphatase ( SHP2 ; also known as PTPN11), leading to morphological aberrations that mirror the changes that are induced by growth factor stimulatio”