| Literature DB >> 15862290 |
Naro Ohashi1, Tatsuo Yamamoto, Chiharu Uchida, Akashi Togawa, Hirotaka Fukasawa, Yoshihide Fujigaki, Sayuri Suzuki, Kyoko Kitagawa, Takayuki Hattori, Toshiaki Oda, Hidetoshi Hayashi, Akira Hishida, Masatoshi Kitagawa.
Abstract
Smad ubiquitination regulatory factor 2 (Smurf2), a ubiquitin ligase for Smads, plays critical roles in the regulation of transforming growth factor-beta (TGF-beta)-Smad signaling via ubiquitin-dependent degradation of Smad2 and Smad7. We found that TGF-beta stimulates Smurf2 expression. TGF-beta activated the Smurf2 promoter in a TGF-beta responsive cell lines, whereas IL-1alpha, PDGF and epidermal growth factor did not. TGF-beta-mediated Smurf2 promoter activation was inhibited by Smad7 or an activin receptor-like kinase 5 inhibitor but not by dominant negative Smad or disruption of Smad-binding elements in the promoter. Moreover, inhibition of the phosphatidil inositol 3 kinase (PI3K)/Akt pathway suppressed TGF-beta-mediated Smurf2 induction. These results suggest that TGF-beta stimulates Smurf2 expression by Smad-independent pathway such as PI3K/Akt pathway via TGF-beta receptor.Entities:
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Year: 2005 PMID： 15862290 DOI： 10.1016/j.febslet.2005.03.069
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124