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Smad2 and Smad3, the intracellular mediators of transforming growth factor β (TGF-β) signaling, are directly phosphorylated by the activated type Ⅰ receptor kinase, and then shuttle from the cytoplasm into the nucleus to regulate target gene expression.Here, we report that the 70-kDa heat-shock protein (HSP70) interacts with Smad2 and decreases TGF-β signal transduction.Ectopic expression of HSP70 prevents receptor-dependent phosphorylation and nuclear translocation of Smad2, and blocks TGF-β-induced epithelial-mesenchymal transition (EMT) in HaCat cells.Our findings reveal an essential role of HSP70 in TGF-β-induced epithelial-mesenchymal transition (EMT) by impeding Smad2 phosphorylation.