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Updated: Jun 28, 2026

RhoC GTPase Activation Assay
Published on: August 22, 2010
E-Cadherin negatively modulates delta-catenin-induced morphological changes and RhoA activity reduction by competing
Hangun Kim1, Minsoo Oh1, Qun Lu2
1College of Pharmacy and Research Institute of Drug Development, Chonnam National University, Bldg. 1-211, 300 Yongbong-dong, Gwangju 500-757, Republic of Korea.
Abstract:
delta-Catenin is a member of the p120-catenin subfamily of armadillo proteins. Here, we describe distinctive features of delta-catenin localization and its association with E-cadherin in HEK293 epithelial cells. In HEK293 cells maintained in low cell densities, approximately 15% of cells overexpressing delta-catenin showed dendrite-like process formation, but there was no detectable change in RhoA activity. In addition, delta-catenin was localized mainly in the cytoplasm and was associated with p190RhoGEF. However, at high cell densities, delta-catenin localization was shifted to the plasma membrane. The association of delta-catenin with E-cadherin was strengthened, whereas its interaction with p190RhoGEF was weakened. In mouse embryonic fibroblast cell, ectopic expression of E-cadherin decreased the effect of delta-catenin on the reduction of RhoA activity as well as on dendrite-like process formation. These results suggest that delta-catenin is more dominantly bound to E-cadherin than to p190RhoGEF, and that delta-catenin's function is dependent on its cellular binding partner.
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