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Cell Growth & Differentiation Vol. 12, 457-463, September 2001
© 2001 American Association for Cancer Research

The Smad Transcriptional Corepressor TGIF Recruits mSin31

David Wotton2, Paul S. Knoepfler, Carol D. Laherty, Robert N. Eisenman and Joan Massagué

Department of Biochemistry and Molecular Genetics and Center for Cell Signaling, 800577 HSC, University of Virginia, Charlottesville, Virginia 22908 [D. W.]; Division of Basis Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109 [P. S. K., C. D. L., R. N. E.]; Cell Biology Program, Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York, New York 10021 [J. M.]

The homeodomain protein TG-interacting factor (TGIF) represses transcription by histone deacetylase-dependent and -independent means. Heterozygous mutations in human TGIF result in holoprosencephaly, a severe genetic disorder affecting craniofacial development, suggesting that TGIF is critical for normal development. After transforming growth factorß (TGFß) stimulation, Smad proteins enter the nucleus and form transcriptional activation complexes or interact with TGIF, which functions as a corepressor. The relative levels of Smad corepressors and coactivators present within the cell may determine the outcome of a TGFß response. We show that TGIF interacts directly with the paired amphipathic {alpha}-helix 2 domain of the mSin3 corepressor, and TGIF recruits mSin3 to a TGFß-activated Smad complex. The mSin3 interaction domain of TGIF has been shown to be essential for repression of a TGFß transcriptional response. Thus, TGIF represents a targeting component of the mSin3 corepressor complex.




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