Helicobacter pylori CagA oncoprotein interacts with SHIP2 to increase its delivery into gastric epithelial cells.
Amino Acid Motifs
Animals
Antigens, Bacterial
/ chemistry
Bacterial Proteins
/ chemistry
Cell Line
Cell Membrane
/ metabolism
Epithelial Cells
/ metabolism
Epithelial-Mesenchymal Transition
Gastric Mucosa
/ metabolism
Helicobacter Infections
/ metabolism
Helicobacter pylori
/ genetics
Humans
Phosphatidylinositol Phosphates
/ metabolism
Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases
/ chemistry
Phosphorylation
Protein Binding
Protein Transport
Protein Tyrosine Phosphatase, Non-Receptor Type 11
/ chemistry
src Homology Domains
Helicobacter pylori
CagA
PI(3,4)P2
SHIP2
gastric cancer
Journal
Cancer science
ISSN: 1349-7006
Titre abrégé: Cancer Sci
Pays: England
ID NLM: 101168776
Informations de publication
Date de publication:
May 2020
May 2020
Historique:
received:
20
11
2019
revised:
11
03
2020
accepted:
12
03
2020
pubmed:
22
3
2020
medline:
2
6
2020
entrez:
22
3
2020
Statut:
ppublish
Résumé
Chronic infection with Helicobacter pylori cagA-positive strains is causally associated with the development of gastric diseases, most notably gastric cancer. The cagA-encoded CagA protein, which is injected into gastric epithelial cells by bacterial type IV secretion, undergoes tyrosine phosphorylation at the Glu-Pro-Ile-Tyr-Ala (EPIYA) segments (EPIYA-A, EPIYA-B, EPIYA-C, and EPIYA-D), which are present in various numbers and combinations in its C-terminal polymorphic region, thereby enabling CagA to promiscuously interact with SH2 domain-containing host cell proteins, including the prooncogenic SH2 domain-containing protein tyrosine phosphatase 2 (SHP2). Perturbation of host protein functions by aberrant complex formation with CagA has been considered to contribute to the development of gastric cancer. Here we show that SHIP2, an SH2 domain-containing phosphatidylinositol 5'-phosphatase, is a hitherto undiscovered CagA-binding host protein. Similar to SHP2, SHIP2 binds to the Western CagA-specific EPIYA-C segment or East Asian CagA-specific EPIYA-D segment through the SH2 domain in a tyrosine phosphorylation-dependent manner. In contrast to the case of SHP2, however, SHIP2 binds more strongly to EPIYA-C than to EPIYA-D. Interaction with CagA tethers SHIP2 to the plasma membrane, where it mediates production of phosphatidylinositol 3,4-diphosphate [PI(3,4)P
Identifiants
pubmed: 32198795
doi: 10.1111/cas.14391
pmc: PMC7226221
doi:
Substances chimiques
Antigens, Bacterial
0
Bacterial Proteins
0
Phosphatidylinositol Phosphates
0
cagA protein, Helicobacter pylori
0
phosphatidylinositol 3,4-diphosphate
0
PTPN11 protein, human
EC 3.1.3.48
Protein Tyrosine Phosphatase, Non-Receptor Type 11
EC 3.1.3.48
INPPL1 protein, human
EC 3.1.3.86
Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases
EC 3.1.3.86
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1596-1606Subventions
Organisme : Japan Society for the Promotion of Science
ID : JP16H06373
Organisme : Japan Society for the Promotion of Science
ID : JP19K08436
Organisme : Max-Planck-Gesellschaft
Informations de copyright
© 2020 The Authors. Cancer Science published by John Wiley & Sons Australia, Ltd on behalf of Japanese Cancer Association.
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