| Literature DB >> 21477782 |
Yihao Li1, Xianjiang Kang, Qiang Wang.
Abstract
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.Entities:
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Year: 2011 PMID： 21477782 DOI： 10.1016/j.jgg.2011.02.001
Source DB: PubMed Journal: J Genet Genomics ISSN： 1673-8527 Impact factor: 4.275