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Originally published In Press as doi:10.1074/jbc.M010815200 on March 6, 2001

J. Biol. Chem., Vol. 276, Issue 21, 18243-18248, May 25, 2001
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Ski-interacting Protein Interacts with Smad Proteins to Augment Transforming Growth Factor-beta -dependent Transcription*

Gary M. LeongDagger §, Nanthakumar SubramaniamDagger , Jonine Figueroa, Judith L. FlanaganDagger , Michael J. Hayman, John A. EismanDagger , and Alexander P. KouzmenkoDagger

From the Dagger  Bone & Mineral Research Program, Garvan Institute of Medical Research, Darlinghurst, New South Wales 2010, Australia and the  Department of Molecular Genetics & Microbiology, State University of New York, Stony Brook, New York 11794

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.

* This work was supported by a National Health and Medical Research Council (NHMRC) grant to the Bone & Mineral Research Program at the Garvan Institute, in part through a NHMRC medical postgraduate scholarship (to G. M. L.), and by National Institutes of Health Public Service Grants CA28146 and CA42573 (to M. J. H).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: Bone & Mineral Research Program, Garvan Inst. of Medical Research, 384 Victoria St., Darlinghurst, New South Wales 2010, Australia. Tel.: 61-2-9295-8247; Fax: 61-2-9295-8241; E-mail: g.leong@garvan.unsw.edu.au.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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