Title : Tyrosine phosphorylation translocates beta-catenin from cell-->cell interface to the cytoplasm, but does not significantly enhance the LEF-1-dependent transactivating function.

Pub. Date : 2001

PMID : 11401329






5 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 Tyrosine phosphorylation translocates beta-catenin from cell-->cell interface to the cytoplasm, but does not significantly enhance the LEF-1-dependent transactivating function. Tyrosine catenin beta 1 Homo sapiens
2 Tyrosine phosphorylation of beta-catenin has been shown to correlate with tumorigenesis, cell migration, and developmental processes. Tyrosine catenin beta 1 Homo sapiens
3 Treatment with a PTPase inhibitor, pervanadate, increased the tyrosine phosphorylation of beta-catenin in a time-dependent manner and led to its relocation from cell-cell interfaces to the cytoplasm. Tyrosine catenin beta 1 Homo sapiens
4 However, tyrosine phosphorylation of beta-catenin does not change its binding affinity to LEF-1 nor enhance cyclin D1 transactivation, a nuclear target of beta-catenin/LEF-1. Tyrosine catenin beta 1 Homo sapiens
5 This result suggests that tyrosine phosphorylation of beta-catenin has effects on the binding to cadherins in the cytoplasm but not on its LEF-1-dependent transactivating function in the nucleus. Tyrosine catenin beta 1 Homo sapiens