کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2049033 | 1074113 | 2010 | 4 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: A newly identified Pirh2 substrate SCYL1-BP1 can bind to MDM2 and accelerate MDM2 self-ubiquitination A newly identified Pirh2 substrate SCYL1-BP1 can bind to MDM2 and accelerate MDM2 self-ubiquitination](/preview/png/2049033.png)
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.Structured summaryMINT-7904819, MINT-7904837, MINT-7904806, MINT-7904715: MDM2 (uniprotkb:Q00987) physically interacts (MI:0915) with SCYL1-BP1 (uniprotkb:Q5T7V8) by anti tag coimmunoprecipitation (MI:0007)MINT-7904857, MINT-7904899: SCYL1-BP1 (uniprotkb:Q5T7V8) physically interacts (MI:0915) with MDM2 (uniprotkb:Q00987) by anti bait coimmunoprecipitation (MI:0006)
Journal: FEBS Letters - Volume 584, Issue 15, 4 August 2010, Pages 3275–3278