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RHOA — SMAD3

Text-mined interactions from Literome

Chen et al., J Biol Chem 2006 : Dominant negative RhoA blocked nuclear translocation of Smad2 and Smad3 because of the inhibition of phosphorylation of both Smads and inhibited Smad dependent SBE promoter activity, whereas constitutively active RhoA significantly enhanced SBE promoter activity
Vardouli et al., FEBS J 2008 : In addition, Smad2 and Smad3 triggered activation of RhoA and RhoB GTPases and long-term actin reorganization in Swiss 3T3 fibroblasts
Lee et al., J Biol Chem 2010 : Consistent with these results, both dominant negative Smad3 and constitutively active Smad7 blocked the cytoplasmic localization of NET1 and inhibited interactions between NET1 and RhoA ... Taken together, our results demonstrate that Smad3 regulates RhoA activation and cytoskeletal reorganization by controlling NET1 in TGF-beta1 induced ARPE-19 cells
Cho et al., Hepatology 2010 (Liver Cirrhosis) : E-cadherin antagonizes transforming growth factor ß1 gene induction in hepatic stellate cells by inhibiting RhoA dependent Smad3 phosphorylation ... Consistently, ECAD was capable of binding p120-ctn, which recruited RhoA ; this prevented TGFß1 from increasing RhoA mediated Smad3 phosphorylation ... Conclusion : Our results demonstrate that ECAD inhibits Smad3/2 phosphorylation by recruiting RhoA to p120-ctn at the p120-ctn binding domain, whereas the loss of ECAD due to cadherin switching promotes the up-regulation of TGFß1 and its target genes, and facilitates liver fibrosis