Grb2 Is a Key Mediator of Helicobacter pylori CagA Protein Activities
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...
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| Veröffentlicht in: | Molecular cell 2002-10, Vol.10 (4), p.745-755 |
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| container_title | Molecular cell |
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| creator | Mimuro, Hitomi Suzuki, Toshihiko Tanaka, Jiro Asahi, Momoyo Haas, Rainer Sasakawa, Chihiro |
| description | 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. |
| doi_str_mv | 10.1016/S1097-2765(02)00681-0 |
| format | Article |
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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
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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
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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.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>12419219</pmid><doi>10.1016/S1097-2765(02)00681-0</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing Animals Antigens, Bacterial Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Cell Division Cell Line Cell Movement Cell Size COS Cells GRB2 Adaptor Protein Helicobacter pylori - genetics Helicobacter pylori - metabolism Humans Mutation Phosphorylation Phosphotyrosine - metabolism Protein Binding Proteins - genetics Proteins - metabolism Signal Transduction |
| title | Grb2 Is a Key Mediator of Helicobacter pylori CagA Protein Activities |
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