Xuyu Yang1, Seong-Ho Lee2. 1. Department of Nutrition and Food Science, College of Agriculture and Natural Resources, University of Maryland, College Park, MD, U.S.A. 2. Department of Nutrition and Food Science, College of Agriculture and Natural Resources, University of Maryland, College Park, MD, U.S.A. slee2000@umd.edu.
Abstract
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. Copyright
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. Copyright
Authors: D Liu; Y Skomorovska; J Song; E Bowler; R Harris; M Ravasz; S Bai; M Ayati; K Tamai; M Koyuturk; X Yuan; Z Wang; Y Wang; R M Ewing Journal: Cancer Biol Ther Date: 2018-08-27 Impact factor: 4.742