SAFB1 interacts with and suppresses the transcriptional activity of p53.
A significant amount of nuclear p53 is found associated with the nuclear matrix in cells that were exposed to genotoxic stress. In this study we identified Scaffold attachment factor B1 (SAFB1), a nuclear matrix-associated protein that binds the scaffold or matrix attachment regions (S/MARs) of genomic DNA, as a novel ... p53-interacting protein. SAFB1 was able to associate with p53 through its C-terminal domain, while significant co-localization of the two proteins was observed in cells treated with 5-fluorouracil or mithramycin. Binding of p53 to SAFB1 had a significant functional outcome, since SAFB1 was shown to suppress p53-mediated reporter gene expression. These data suggest that nuclear matrix-associated proteins may play a critical role in regulating p53 localization and activity.
Mesh Terms:
Antineoplastic Agents, Cell Nucleus, Fluorouracil, Green Fluorescent Proteins, HEK293 Cells, Hep G2 Cells, Humans, Immunoblotting, K562 Cells, Matrix Attachment Region Binding Proteins, Microscopy, Fluorescence, Nuclear Matrix-Associated Proteins, Plicamycin, Protein Binding, Protein Transport, Protein-Serine-Threonine Kinases, RNA Interference, Receptors, Estrogen, Transcriptional Activation, Transfection, Tumor Suppressor Protein p53, Two-Hybrid System Techniques
Antineoplastic Agents, Cell Nucleus, Fluorouracil, Green Fluorescent Proteins, HEK293 Cells, Hep G2 Cells, Humans, Immunoblotting, K562 Cells, Matrix Attachment Region Binding Proteins, Microscopy, Fluorescence, Nuclear Matrix-Associated Proteins, Plicamycin, Protein Binding, Protein Transport, Protein-Serine-Threonine Kinases, RNA Interference, Receptors, Estrogen, Transcriptional Activation, Transfection, Tumor Suppressor Protein p53, Two-Hybrid System Techniques
FEBS Lett.
Date: Jan. 03, 2011
PubMed ID: 21130767
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