RRC ID 961
Author Mimuro H, Suzuki T, Tanaka J, Asahi M, Haas R, Sasakawa C.
Title Grb2 is a key mediator of helicobacter pylori CagA protein activities.
Journal Mol Cell
Abstract CagA delivered from Helicobacter pylori into gastric epithelial cells undergoes tyrosine phosphorylation and induces host cell morphological changes. Here we show that CagA can interact with Grb2 both in vitro and in vivo, which results in the activation of the Ras/MEK/ERK pathway and leads to cell scattering as well as proliferation. Importantly, this ability of CagA is independent from the tyrosine phosphorylation, which occurs within the five repeated EPIYA sequences (PY region) of CagA. However, the PY region appears to be indispensable for the Grb2 binding and induction of the cellular responses. Thus, intracellular CagA via its binding to Grb2 may act as a transducer for stimulating growth factor-like downstream signals which lead to cell morphological changes and proliferation, the causes of H. pylori-induced gastric hyperplasia.
Volume 10(4)
Pages 745-55
Published 2002-10-1
DOI 10.1016/s1097-2765(02)00681-0
PII S1097-2765(02)00681-0
PMID 12419219
MeSH Adaptor Proteins, Signal Transducing* Animals Antigens, Bacterial* Bacterial Proteins / chemistry Bacterial Proteins / genetics Bacterial Proteins / metabolism* COS Cells Cell Division Cell Line Cell Movement Cell Size GRB2 Adaptor Protein Helicobacter pylori / genetics Helicobacter pylori / metabolism* Humans Mutation Phosphorylation Phosphotyrosine / metabolism Protein Binding Proteins / genetics Proteins / metabolism* Signal Transduction
IF 15.584
Times Cited 267
WOS Category BIOCHEMISTRY & MOLECULAR BIOLOGY CELL BIOLOGY
Resource
Pathogenic microorganisms IID 3022(ATCC 43579)? IID 3023(NCTC 11637)? IID 6171(26695)?