Anticancer research · 2016
Identification of ESE1 as a β-Catenin Binding Protein.
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Yang Xuyu, Lee Seong-Ho
Аннотация
BACKGROUND/AIM: β-Catenin regulates cell-cell adhesion and gene transcription and acts as a master switch that controls proliferation in several types of cancer. ESE1 is an epithelium-restricted transcription factor and its multiple domain structure predicts its interaction with other proteins with diverse cellular functions. Here, for the first time, we report that endogenous β-catenin binds to and co-localizes with endogenous ESE1 in the cytoplasm.
MATERIALS AND METHODS: The binding sites were mapped to E26 transformation-specific (ETS) domain at carboxyl terminus of ESE1 and N-terminus of β-catenin.
RESULTS: We found that C-terminus of ESE1 also binds to α-catenin and that ESE1/β-catenin interaction was abrogated by knockdown of either β-catenin or α-catenin.
CONCLUSION: The data suggest that interactions between ESE1 and β-/α-catenins might be a mechanism by which the ESE1 protein determines the β-catenin function and tumorigenesis.
MATERIALS AND METHODS: The binding sites were mapped to E26 transformation-specific (ETS) domain at carboxyl terminus of ESE1 and N-terminus of β-catenin.
RESULTS: We found that C-terminus of ESE1 also binds to α-catenin and that ESE1/β-catenin interaction was abrogated by knockdown of either β-catenin or α-catenin.
CONCLUSION: The data suggest that interactions between ESE1 and β-/α-catenins might be a mechanism by which the ESE1 protein determines the β-catenin function and tumorigenesis.