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

Hideaki Higashi, Ryouhei Tsutsumi, Syuichi Muto, Toshiro Sugiyama, Takeshi Azuma, Masahiro Asaka, Masanori Hatakeyama

Research output: Contribution to journalArticlepeer-review

752 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)683-686
Number of pages4
JournalScience
Volume295
Issue number5555
DOIs
Publication statusPublished - 2002 Jan 25
Externally publishedYes

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'SHP-2 tyrosine phosphatase as an intracellular target of Helicobacter pylori CagA protein'. Together they form a unique fingerprint.

Cite this