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Ribosomal proteins RPL37, RPS15 and RPS20 regulate the Mdm2-p53-MdmX network

Daftuar, Lilyn ; Zhu, Yan ; Jacq, Xavier ; Prives, Carol Hofmann, Thomas G.

PloS one, 2013-07, Vol.8 (7), p.e68667-e68667 [Periódico revisado por pares]

United States: Public Library of Science

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Título:
Ribosomal proteins RPL37, RPS15 and RPS20 regulate the Mdm2-p53-MdmX network
Autor: Daftuar, Lilyn ; Zhu, Yan ; Jacq, Xavier ; Prives, Carol
Hofmann, Thomas G.
Assuntos: Apoptosis ; Biology ; Biosynthesis ; Cancer ; Cell Cycle ; Cell death ; Cell Line, Tumor ; Evolution ; Gene expression ; Health aspects ; Health risks ; Humans ; Immunoprecipitation ; Ligases ; MDM2 protein ; Medicine ; Mutation ; Nucleoli ; Null cells ; p53 Protein ; Plasmids ; Protein Binding ; Proteins ; Proto-Oncogene Proteins c-mdm2 - genetics ; Proto-Oncogene Proteins c-mdm2 - metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Ribosomal proteins ; Ribosomal Proteins - genetics ; Ribosomal Proteins - metabolism ; Signal transduction ; Signaling ; Stabilization ; Tumor proteins ; Tumor Suppressor Protein p53 - genetics ; Tumor Suppressor Protein p53 - metabolism ; Two-Hybrid System Techniques ; Ubiquitin ; Ubiquitin-protein ligase
É parte de: PloS one, 2013-07, Vol.8 (7), p.e68667-e68667
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Competing Interests: XJ was an employee of Hybrigenics at the time of this study. There are no patents, products in development or marketed products to declare. This does not alter the authors' adherence to all the PLOS ONE policies on sharing data and materials.
Current address: MISSION Therapeutics Ltd, Cambridge, United Kingdom
Conceived and designed the experiments: LD YZ CP. Performed the experiments: LD YZ. Analyzed the data: LD YZ CP. Contributed reagents/materials/analysis tools: XJ. Wrote the paper: LD YZ CP.
Descrição: Changes to the nucleolus, the site of ribosome production, have long been linked to cancer, and mutations in several ribosomal proteins (RPs) have been associated with an increased risk for cancer in human diseases. Relevantly, a number of RPs have been shown to bind to MDM2 and inhibit MDM2 E3 ligase activity, leading to p53 stabilization and cell cycle arrest, thus revealing a RP-Mdm2-p53 signaling pathway that is critical for ribosome biogenesis surveillance. Here, we have identified RPL37, RPS15, and RPS20 as RPs that can also bind Mdm2 and activate p53. We found that each of the aforementioned RPs, when ectopically expressed, can stabilize both co-expressed Flag-tagged Mdm2 and HA-tagged p53 in p53-null cells as well as endogenous p53 in a p53-containing cell line. For each RP, the mechanism of Mdm2 and p53 stabilization appears to be through inhibiting the E3 ubiquitin ligase activity of Mdm2. Interestingly, although they are each capable of inducing cell death and cell cycle arrest, these RPs differ in the p53 target genes that are regulated upon their respective introduction into cells. Furthermore, each RP can downregulate MdmX levels but in distinct ways. Thus, RPL37, RPS15 and RPS20 regulate the Mdm2-p53-MdmX network but employ different mechanisms to do so.
Editor: United States: Public Library of Science
Idioma: Inglês

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Ribosomal proteins RPL37, RPS15 and RPS20 regulate the Mdm2-p53-MdmX network

Daftuar, Lilyn ; Zhu, Yan ; Jacq, Xavier ; Prives, Carol Hofmann, Thomas G.

United States: Public Library of Science

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