IndraLab

Statements


CTNNB1 bound to CDH1 inhibits CTNNB1. 10 / 10
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"The CagA and E-cadherin interaction impairs the complex formation between E-cadherin and beta-catenin, causing cytoplasmic and nuclear accumulation of beta-catenin."

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"Hence, a reduced binding affinity between beta-catenin and E-cadherin is expected to increase the signaling pool of beta-catenin, possibly leading to enhanced nuclear signaling."

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"When subjected to mechanical strain, β-catenin and E-cadherin interactions are disrupted, causing a dissociation of the complex and subsequent translocation of β-catenin into the nucleus."

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"In CAC, E-cadherin forms a complex with beta-catenin and in combination with the actin cytoskeleton prevents nuclear translocation of beta-catenin, thus regulating the activity of the Wnt and catenin signaling pathways [XREF_BIBR]."

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"Indeed, disruption of E-cadherin and beta-catenin complexes leads to the loss of epithelial polarization and allows nuclear translocation of beta-catenin."

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"E-cadherin binding to beta-catenin prevents nuclear localization of beta-catenin and beta-catenin and LEF-1-mediated transactivation [XREF_BIBR, XREF_BIBR]."

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"c-Src kinase-mediated phosphorylation of β-catenin at Y654 disrupts the interaction between β-catenin and E-cadherin and causes redistribution of β-catenin from the AJ to other locations [30] ."

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"However, upon infection with CagA positive H. pylori strains, CagA will become competitive in combination with E-cadherin and disrupt complex formation between E-cadherin and beta-catenin, causing cytoplasmic and nuclear accumulation of beta-catenin."

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"Binding of beta-catenin and E-cadherin at the cell junction is indicative of the antagonism of the Wnt pathway restricting nuclear translocation of beta-catenin XREF_BIBR."

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"In the stomach, CagA physically interacts with E-cadherin and impairs the complex formation between E-cadherin and beta-catenin, causing cytoplasmic and nuclear accumulation of beta-catenin."