Title : Regulation of E-cadherin/Catenin association by tyrosine phosphorylation.

Pub. Date : 1999 Dec 17

PMID : 10593980






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Transient transfections of different mutants demonstrated that Tyr-654 is phosphorylated in conditions in which adherens junctions are disrupted and evidenced that binding of beta-catenin to E-cadherin in vivo is controlled by phosphorylation of beta-catenin Tyr-654. Tyrosine catenin beta 1 Homo sapiens
2 Transient transfections of different mutants demonstrated that Tyr-654 is phosphorylated in conditions in which adherens junctions are disrupted and evidenced that binding of beta-catenin to E-cadherin in vivo is controlled by phosphorylation of beta-catenin Tyr-654. Tyrosine catenin beta 1 Homo sapiens
3 Transient transfections of different mutants demonstrated that Tyr-654 is phosphorylated in conditions in which adherens junctions are disrupted and evidenced that binding of beta-catenin to E-cadherin in vivo is controlled by phosphorylation of beta-catenin Tyr-654. Tyrosine catenin beta 1 Homo sapiens