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RHOA — SMAD2

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Intact Interaction: SMAD2 — RHOA (physical association, display technology) Miyamoto-Sato et al., PloS one 2010
• IRef Intact Interaction: SMAD2 — RHOA (physical association, tandem affinity purification) Miyamoto-Sato et al., PloS one 2010

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
Lu et al., J Appl Physiol 2006 : Transforming growth factor-beta1 induced endothelial barrier dysfunction involves Smad2 dependent p38 activation and subsequent RhoA activation ... In this study, we hypothesized that TGF-beta1 induced changes in endothelial monolayer permeability and in p38 and RhoA activation are dependent on Smad2 signaling
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
Cho et al., Hepatology 2010 (Liver Cirrhosis) : 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