The mSin3 interaction domain (SID) is an interaction domain which is present on several transcriptional repressor proteins including TGFβ (transforming growth factor β) and Mad. It interacts with the paired amphipathic alpha-helix 2 (PAH2) domain of mSin3, a transcriptional repressor domain that is attached to transcription repressor proteins such as the mSin3A corepressor.
Action of histone deacetylase 1 and 2 (HDAC1/2) is induced by the interaction of mSin3A with a multi-protein complex containing HDAC1/2. Transcription is also repressed by histone deacetylase-independent means.
External links edit
- Wotton D, Knoepfler PS, Laherty CD, Eisenman RN, Massagué J (September 2001). "The Smad transcriptional corepressor TGIF recruits mSin3". Cell Growth Differ. 12 (9): 457–63. PMID 11571228.
- A 13-Amino Acid Amphipathic α-Helix Is Required for the Functional Interaction between the Transcriptional Repressor Mad1 and mSin3A
- Zhang JS, Moncrieffe MC, Kaczynski J, Ellenrieder V, Prendergast FG, Urrutia R (August 2001). "A conserved alpha-helical motif mediates the interaction of Sp1-like transcriptional repressors with the corepressor mSin3A". Mol. Cell. Biol. 21 (15): 5041–9. doi:10.1128/MCB.21.15.5041-5049.2001. PMC 87230. PMID 11438660.
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