ArticleFEBS letters2010
A newly identified Pirh2 substrate SCYL1-BP1 can bind to MDM2 and accelerate MDM2 self-ubiquitination.
Article in FEBS letters, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- Targeting the p53 signaling pathway in cancers: Molecular mechanisms and clinical studies.MedComm · 2023Review
- The Role of E3 Ligase Pirh2 in Disease.Cells · 2022Review
- The Close Relationship between the Golgi Trafficking Machinery and Protein Glycosylation.Cells · 2020Review
- GORAB promotes embryonic lung maturation through antagonizing AKT phosphorylation, versican expression, and mesenchymal cell migration.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Gorab Is Required for Dermal Condensate Cells to Respond to Hedgehog Signals during Hair Follicle Morphogenesis.The Journal of investigative dermatology · 2016Review
- Transcriptional profiling and dynamical regulation analysis identify potential kernel target genes of SCYL1-BP1 in HEK293T cells.Molecules and cells · 2014Article
- SCYL1BP1 modulates neurite outgrowth and regeneration by regulating the Mdm2/p53 pathway.Molecular biology of the cell · 2012Article
- HDM2 antagonist MI-219 (spiro-oxindole), but not Nutlin-3 (cis-imidazoline), regulates p53 through enhanced HDM2 autoubiquitination and degradation in human malignant B-cell lymphomas.Journal of hematology & oncology · 2012Article
- Pirh2 RING-finger E3 ubiquitin ligase: its role in tumorigenesis and cancer therapy.FEBS letters · 2012Review
- A novel oncoprotein Pirh2: rising from the shadow of MDM2.Cancer science · 2011Review
- Mdm2 links genotoxic stress and metabolism to p53.Protein & cell · 2010Review
- Overexpression of SCYL1-BP1 stabilizes functional p53 by suppressing MDM2-mediated ubiquitination.FEBS letters · 2010Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.