Single-stranded DNA-binding proteins regulate the abundance of LIM domain and LIM domain-binding proteins The LIM domain-binding protein Ldb1 is an essential cofactor of LIM-homeodomain (LIM-HD) and LIM-only (LMO) proteins in development. The stoichiometry of L... Z Xu,X Meng,Y Cai,......
The MH1 domains of R-SMADs (except full-length SMAD2) and SMAD4 have a DNA binding domain, enabling them to interact directly with target genes to regulate transcription. SMAD3 and SMAD4 can bind a simple DNA sequence, GTCT (or its reverse-complement, AGAC). However, this binding is ...
Our results identify a new co-factor for HOX group 13 proteins and suggest that HOX proteins may modulate Smad-mediated transcriptional activity through protein–protein interactions without the requirement for HOX monomeric DNA-binding capability. 展开 关键词: HOX ...
Interestingly, putative SMAD2/3/4 binding sites were found in the promoter regions of all five genes encoding these DSB repair proteins (Figure 6F). Quantitative chromatin immunoprecipitation (ChIP) analysis indicated that SMAD3 binds to these promoters (Figure 6G), and luciferase-based ...
Further investigations through the residue/base motion correlation and DNA dynamics analyses predicted that the binding of Smad4 protein to DNA molecule in the heteromeric Smad4+DNA+Smad1/3 model induces an allosteric communication from the Smad4-DNA interface to Smad1/Smad3-DNA interface via DNA...
phosphorylated in response to BMP (Bone Morphogenetic Protein). This C-terminal phosphorylation allows R-Smad binding to Co-Smad, Smad4, and translocation to the nucleus where they regulate TGF-beta target genes. Smad6 and Smad7 belong to the I-Smad which bind to the type I receptor or ...
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The glycine binding site of the N-methyl-D-aspartate receptor subunit NR1: identification of novel determinants of co-agonist potentiation in the extracell... The N-methyl-D-aspartate (NMDA) subtype of ionotropic glutamate receptors is a heterooligomeric membrane protein composed of homologous subuni...
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Activated Smad3 oligomerizes with Smad4 upon TGF beta stimulation and translocates as a complex into the nucleus, allowing its binding to DNA and transcription factors. Phosphorylation of the two TGF beta dependent serines 423 and 425 in the C terminus of Smad3 is critical for Smad3 ...