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Smad6 is a Smad1/5-induced smad inhibitor. Characterization of bone morphogenetic protein-responsive element in the mouse Smad6 promoter 总被引:7,自引:0,他引:7
Ishida W Hamamoto T Kusanagi K Yagi K Kawabata M Takehara K Sampath TK Kato M Miyazono K 《The Journal of biological chemistry》2000,275(9):6075-6079
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Regulation of Smad7 promoter by direct association with Smad3 and Smad4 总被引:26,自引:0,他引:26
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Mechanism of a transcriptional cross talk between transforming growth factor-beta-regulated Smad3 and Smad4 proteins and orphan nuclear receptor hepatocyte nuclear factor-4 总被引:5,自引:0,他引:5
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Chou WC Prokova V Shiraishi K Valcourt U Moustakas A Hadzopoulou-Cladaras M Zannis VI Kardassis D 《Molecular biology of the cell》2003,14(3):1279-1294
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Direct binding of Smad1 and Smad4 to two distinct motifs mediates bone morphogenetic protein-specific transcriptional activation of Id1 gene. 总被引:11,自引:0,他引:11
Teresa López-Rovira Elisabet Chalaux Joan Massagué Jose Luis Rosa Francesc Ventura 《The Journal of biological chemistry》2002,277(5):3176-3185
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Baburajendran N Jauch R Tan CY Narasimhan K Kolatkar PR 《Nucleic acids research》2011,39(18):8213-8222
Smad proteins form multimeric complexes consisting of the 'common partner' Smad4 and receptor regulated R-Smads on clustered DNA binding sites. Deciphering how pathway specific Smad complexes multimerize on DNA to regulate gene expression is critical for a better understanding of the cis-regulatory logic of TGF-β and BMP signaling. To this end, we solved the crystal structure of the dimeric Smad4 MH1 domain bound to a palindromic Smad binding element. Surprisingly, the Smad4 MH1 forms a constitutive dimer on the SBE DNA without exhibiting any direct protein-protein interactions suggesting a DNA mediated indirect readout mechanism. However, the R-Smads Smad1, Smad2 and Smad3 homodimerize with substantially decreased efficiency despite pronounced structural similarities to Smad4. Therefore, intricate variations in the DNA structure induced by different Smads and/or variant energetic profiles likely contribute to their propensity to dimerize on DNA. Indeed, competitive binding assays revealed that the Smad4/R-Smad heterodimers predominate under equilibrium conditions while R-Smad homodimers are least favored. Together, we present the structural basis for DNA recognition by Smad4 and demonstrate that Smad4 constitutively homo- and heterodimerizes on DNA in contrast to its R-Smad partner proteins by a mechanism independent of direct protein contacts. 相似文献