RT Journal Article
SR Electronic
T1 Identification of ESE1 as a β-Catenin Binding Protein
JF Anticancer Research
JO Anticancer Res
FD International Institute of Anticancer Research
SP 2697
OP 2703
VO 36
IS 6
A1 XUYU YANG
A1 SEONG-HO LEE
YR 2016
UL http://ar.iiarjournals.org/content/36/6/2697.abstract
AB 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.