ExpSup: CagA Physically Interacts with E-cadherin in Tyrosine-phosphorylation Independent Manner

Murata-Kamiya et al., 2007 showed that E-cadherin physically interacts with CagA protein using co-immunoprecipitation in cell lysate prepared from MKN-28 cell line either stably expressing wild-type CagA or phospho-resistant CagA mutant. Since they could co-immunoprecipitate E-cadherin from cell lysate expressing phospho-resistant CagA mutant, they concluded that CagA interaction with E-cadherin is independent of CagA phosphorylation.

Method: Co-immunoprecipitation using HA (hemagglutinin)-tag antibody and detection using E-cadherin and HA-tag antibodies
Cell line: MKN-28 cell line stably expressing either HA-tagged wild-type CagA or HA-tagged phospho-resistant CagA mutant

REFERENCES:

Murata-Kamiya et al., 2007. Helicobacter pylori CagA interacts with E-cadherin and deregulates the beta-catenin signal that promotes intestinal transdifferentiation in gastric epithelial cells. Oncogene. 26(32), 4617-4626. PMID-17237808; Full Text Links: Nature 

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