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FEBS Lett. 2010 Aug 4;584(15):3275-8. doi: 10.1016/j.febslet.2010.06.027. Epub 2010 Jun 23.

A newly identified Pirh2 substrate SCYL1-BP1 can bind to MDM2 and accelerate MDM2 self-ubiquitination.

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1
State Key Laboratory of Genetic Engineering, Fudan University, Shanghai, China.

Abstract

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.

PMID:
20598683
PMCID:
PMC3798065
DOI:
10.1016/j.febslet.2010.06.027
[Indexed for MEDLINE]
Free PMC Article
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