S100 proteins interact with the N-terminal domain of MDM2.
S100 proteins interact with the transactivation domain and the C-terminus of p53. Further, S100B has been shown to interact with MDM2, a central negative regulator of p53. Here, we show that S100B bound directly to the folded N-terminal domain of MDM2 (residues 2-125) by size exclusion chromatography and surface plasmon ... resonance experiments. This interaction with MDM2 (2-125) is a general feature of S100 proteins; S100A1, S100A2, S100A4 and S100A6 also interact with MDM2 (2-125). These interactions with S100 proteins do not result in a ternary complex with MDM2 (2-125) and p53. Instead, we observe the ability of a subset of S100 proteins to disrupt the extent of MDM2-mediated p53 ubiquitylation in vitro.
Mesh Terms:
Binding Sites, Biotinylation, Chromatography, Gel, Humans, Light, Protein Binding, Protein Structure, Tertiary, Proto-Oncogene Proteins c-mdm2, S100 Proteins, Scattering, Radiation, Surface Plasmon Resonance, Tumor Suppressor Protein p53, Ubiquitination
Binding Sites, Biotinylation, Chromatography, Gel, Humans, Light, Protein Binding, Protein Structure, Tertiary, Proto-Oncogene Proteins c-mdm2, S100 Proteins, Scattering, Radiation, Surface Plasmon Resonance, Tumor Suppressor Protein p53, Ubiquitination
FEBS Lett.
Date: Aug. 04, 2010
PubMed ID: 20591429
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