A newly identified Pirh2 substrate SCYL1-BP1 can bind to MDM2 and accelerate MDM2 self-ubiquitination.
The SCY1-like 1 binding protein 1 (SCYL1-BP1) protein was identified as an interacting partner of E3 ligase p53-induced RING H2 protein (Pirh2) and mouse double minute gene number 2 (MDM2) by yeast two-hybrid screening. Further investigation suggested there are two interactions involved in different mechanisms. SCYL1-BP1 can be ubiquitinated and ... degraded by Pirh2 but not by MDM2, which suggests that SCYL1-BP1 can be regulated by Pirh2. On the other hand, while SCYL1-BP1 binds to ubiquitin E3 ligase MDM2, it promotes MDM2 self-ubiquitination and results in a reduction of MDM2 protein level.
Mesh Terms:
Animals, Cell Line, Down-Regulation, Humans, Mice, Proteasome Endopeptidase Complex, Protein Binding, Protein Structure, Tertiary, Proto-Oncogene Proteins c-mdm2, Substrate Specificity, Syntenins, Ubiquitin-Protein Ligases, Ubiquitination
Animals, Cell Line, Down-Regulation, Humans, Mice, Proteasome Endopeptidase Complex, Protein Binding, Protein Structure, Tertiary, Proto-Oncogene Proteins c-mdm2, Substrate Specificity, Syntenins, Ubiquitin-Protein Ligases, Ubiquitination
FEBS Lett.
Date: Aug. 04, 2010
PubMed ID: 20598683
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- Interactions 3
- PTM Genes 2