A newly identified Pirh2 substrate SCYL1-BP1 can bind to MDM2 and accelerate MDM2 self-ubiquitination |
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| Authors: | Jing Yan Di Zhang Huili Shi Keke Huo |
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| Institution: | a State Key Laboratory of Genetic Engineering, Fudan University, Shanghai, China
b Institute of Biotechnology, University of Texas Health Science Center, San Antonio, TX, USA |
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| 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.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) |
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| Keywords: | SCY1-like 1 binding protein 1 Mouse double minute gene number 2 p53-Induced RING H2 protein Protein degradation Ubiquitination |
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