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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Ski-interacting protein interacts with Smad proteins to augment transforming growth factor-beta-dependent transcription.

Transforming growth factor-beta (TGF-beta) signaling requires the action of Smad proteins in association with other DNA-binding factors and coactivator and corepressor proteins to modulate target gene transcription. Smad2 and Smad3 both associate with the c-Ski and Sno oncoproteins to repress transcription of Smad target genes via recruitment of a nuclear corepressor complex. Ski-interacting protein (SKIP), a nuclear hormone receptor coactivator, was examined as a possible modulator of transcriptional regulation of the TGF-beta-responsive promoter from the plasminogen activator inhibitor gene-1. SKIP augmented TGF-beta-dependent transactivation in contrast to Ski/ Sno-dependent repression of this reporter. SKIP interacted with Smad2 and Smad3 proteins in vivo in yeast and in mammalian cells through a region of SKIP between amino acids 201-333. In vitro, deletion of the Mad homology domain 2 (MH2) domain of Smad3 abrogated SKIP binding, like Ski/ Sno, but the MH2 domain of Smad3 alone was not sufficient for protein-protein interaction. Overexpression of SKIP partially overcame Ski/ Sno-dependent repression, whereas Ski/ Sno overexpression attenuated SKIP augmentation of TGF-beta-dependent transcription. Our results suggest a potential mechanism for transcriptional control of TGF-beta signaling that involves the opposing and competitive actions of SKIP and Smad MH2-interacting factors, such as Ski and/or Sno. Thus, SKIP appears to modulate both TGF-beta and nuclear hormone receptor signaling pathways.[1]


  1. Ski-interacting protein interacts with Smad proteins to augment transforming growth factor-beta-dependent transcription. Leong, G.M., Subramaniam, N., Figueroa, J., Flanagan, J.L., Hayman, M.J., Eisman, J.A., Kouzmenko, A.P. J. Biol. Chem. (2001) [Pubmed]
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