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The oncoprotein Ski represses transforming growth factor (TGF)-beta signaling in an N-CoR-independent manner. However, the molecular mechanism(s) underlying this event has not been elucidated. Here, we identify an additional domain in Ski that mediates interaction with Smad3 which is important for this repression. This domain is distinct from the previously reported N-terminal Smad3 binding domain in Ski. Individual alanine substitution of several residues in the domain significantly affected Ski-Smad3 interaction. Furthermore, combined mutations within this domain, together with those in the previously identified Smad3 binding domain, can completely abolish the interaction of Ski with Smad3, while mutation in each domain alone retained partial interaction. By introducing those mutations that abolish direct interaction with Smad3 or Smad4 individually, or in combination, we show that interaction of Ski with either Smad3 or Smad4 is sufficient for Ski-mediated repression of TGF-beta signaling. Furthermore our results clearly demonstrate that Ski does not disrupt Smad3-Smad4 heteromer formation, and recruitment of Ski to the Smad3/4 complex through binding to either Smad3 or Smad4 is both necessary and sufficient for repression. 相似文献
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C Venot M Maratrat C Dureuil E Conseiller L Bracco L Debussche 《The EMBO journal》1998,17(16):4668-4679
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Hewitt GF Strunk BS Margulies C Priputin T Wang XD Amey R Pabst BA Kosman D Reinitz J Arnosti DN 《Development (Cambridge, England)》1999,126(6):1201-1210
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The human transcriptional repressor protein NAB1: expression and biological activity 总被引:4,自引:0,他引:4
Thiel G Kaufmann K Magin A Lietz M Bach K Cramer M 《Biochimica et biophysica acta》2000,1493(3):289-301
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Delage-Mourroux R Martini PG Choi I Kraichely DM Hoeksema J Katzenellenbogen BS 《The Journal of biological chemistry》2000,275(46):35848-35856