S100 proteins interact with the N-terminal domain of MDM2.
FEBS Lett
; 584(15): 3269-74, 2010 Aug 04.
Article
em En
| MEDLINE
| ID: mdl-20591429
ABSTRACT
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.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas S100
/
Proteínas Proto-Oncogênicas c-mdm2
Idioma:
En
Ano de publicação:
2010
Tipo de documento:
Article