ArticleThe Journal of biological chemistry2011
Hydrophilic residues are crucial for ribosomal protein L11 (RPL11) interaction with zinc finger domain of MDM2 and p53 protein activation.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 33 citations in OpenAlex.
- The MDM2-p53 Axis in Osteosarcoma: Current Understanding of Regulatory Mechanisms and Targeted Therapeutic Strategies.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Deep Sequencing Reveals Novel Mutations inInternational journal of molecular sciences · 2025Article
- Structure and function of MDM2 and MDM4 in health and disease.The Biochemical journal · 2025Review
- Transcriptomic profiling of diabetic retinopathy: insights into RPL11 and bisphenol A.Frontiers in endocrinology · 2025Article
- Single-Cell Sequence and Machine Learning Identify a CD79A+B Cells-Related Transcriptional Signature for Predicting Clinical Outcomes and Immune Microenvironment in Breast Cancer.Cancer informatics · 2025Article
- Silencing Ribosomal Protein L22 Promotes Proliferation and Migration, and Inhibits Apoptosis of Gastric Cancer Cells by Regulating the Murine Double Minute 2-Protein 53 (MDM2-p53) Signaling Pathway.Medical science monitor : international medical journal of experimental and clinical research · 2021Article
- BOP1 Knockdown Attenuates Neointimal Hyperplasia by Activating p53 and Inhibiting Nascent Protein Synthesis.Oxidative medicine and cellular longevity · 2021Article
- RBM10, a New Regulator of p53.Cells · 2020Review
- Article
- An improved method for the heterologous production of soluble human ribosomal proteins in Escherichia coli.Scientific reports · 2019Article
- A single synonymous mutation determines the phosphorylation and stability of the nascent protein.Journal of molecular cell biology · 2019Article
- Cancer-mutated ribosome protein L22 (RPL22/eL22) suppresses cancer cell survival by blocking p53-MDM2 circuit.Oncotarget · 2017Article
- Mdm2 mediates FMRP- and Gp1 mGluR-dependent protein translation and neural network activity.Human molecular genetics · 2017Article
- Functional characterization of p53 pathway components in the ancient metazoan Trichoplax adhaerens.Scientific reports · 2016Article
- Role of ribosomal protein mutations in tumor development (Review).International journal of oncology · 2016Review
- RRP12 is a crucial nucleolar protein that regulates p53 activity in osteosarcoma cells.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Article
- TFIIS.h, a new target of p53, regulates transcription efficiency of pro-apoptotic bax gene.Scientific reports · 2016Article
- Structure of human MDM2 complexed with RPL11 reveals the molecular basis of p53 activation.Genes & development · 2015Article
- Ribosomal proteins L11 and L5 activate TAp73 by overcoming MDM2 inhibition.Cell death and differentiation · 2015Article
- Ribosomal proteins and human diseases: pathogenesis, molecular mechanisms, and therapeutic implications.Medicinal research reviews · 2015Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Ribosomal protein L11 (RPL11) has been shown to activate p53 by binding to MDM2 and negating its p53 suppression activity in response to ribosomal stress. Although a mutation at Cys-305 within the zinc finger domain of MDM2 has been shown to drastically impair MDM2 interaction with RPL11 and thus escapes the inhibition by this ribosomal protein, it still remains elusive whether RPL11 inactivates MDM2 via direct action on this zinc finger domain and what is the chemical nature of this specific interaction. To define the roles of the MDM2 zinc finger in association with RPL11, we conducted hydrogen-deuterium exchange mass spectrometry, computational modeling, circular dichroism, and mutational analyses of the zinc finger domain of MDM2 and human RPL11. Our study reveals that RPL11 forms a stable complex with MDM2 in vitro through direct contact with its zinc finger. This binding is disrupted by single mutations of non-cysteine amino acids within the zinc finger domain of MDM2. Basic residues in RPL11 are crucial for the stable binding and RPL11 suppression of MDM2 activity toward p53. These results provide the first line of evidence for the specific interaction between RPL11 and the zinc finger of MDM2 via hydrophilic residues as well as a molecular foundation for better understanding RPL11 inhibition of MDM2 function.
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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.