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Open AccessJournal ArticleDOI

Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain.

TLDR
DNA pull-down assays using a 7,8-dihydro-8-oxoguanine duplex oligonucleotide as a substrate found that RPS3 acted as a scaffold for the additional binding of MDM2 and p53, suggesting that R PS3 interacts with important proteins involved in maintaining genomic integrity.
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This article is published in DNA Repair.The article was published on 2009-10-02 and is currently open access. It has received 146 citations till now. The article focuses on the topics: Proximity ligation assay & Ubiquitin ligase.

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Ribosomal proteins: functions beyond the ribosome

TL;DR: The current understanding of how ribosomal stress provokes the accumulation of ribosome-free Ribosomal proteins, as well as the ribosomesome-independent functions of ribOSomal proteins in tumorigenesis, immune signaling, and development are overviewed.
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Ribosome biogenesis surveillance: probing the ribosomal protein-Mdm2-p53 pathway.

TL;DR: This review will clarify how disruption to three major components of ribosome biogenesis can trigger nucleolar stress and activate p53, thereby lending support to a RP-Mdm2-p53 ribosom biogenesis surveillance pathway.
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Targeting the nucleolus for cancer intervention

TL;DR: Extra-ribosomal functions of the nucleolus position it as a central integrator of cellular proliferation and stress signaling, and are emerging as important mechanisms for modulating how oncogenes and tumor suppressors operate in normal and malignant cells.
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Nucleolar stress with and without p53

TL;DR: The human ribosomopathies, syndromes in which ribosome biogenesis or function are impaired leading to birth defects or bone narrow failures, are summarized and the significance of p53 activation upon nucleolar stress resulting in cell cycle arrest or apoptosis cannot be understated.
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The nucleolus: an emerging target for cancer therapy

TL;DR: The largely untapped potential of the nucleolus and ribosomal gene transcription are reviewed as exciting new targets for cancer therapy.
References
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Journal ArticleDOI

In vivo activation of the p53 pathway by small-molecule antagonists of MDM2.

TL;DR: In this article, the authors identify potent and selective small-molecule antagonists of MDM2 and confirm their mode of action through the crystal structures of complexes, leading to cell cycle arrest, apoptosis, and growth inhibition of human tumor xenografts.
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Mdm2 promotes the rapid degradation of p53

TL;DR: It is proposed that the Mdm2-promoted degradation of p53 provides a new mechanism to ensure effective termination of the p53 signal.
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Blinded by the Light: The Growing Complexity of p53

TL;DR: Control of p53's transcriptional activity is crucial for determining which p53 response is activated, a decision that must be understood if the next generation of drugs that selectively activate or inhibit p53 are to be exploited efficiently.
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Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53

TL;DR: The data suggest that the MDM2 protein, which is induced by p53, functions as a ubiquitin ligase, E3, in human papillomavirus‐uninfected cells which do not have E6 protein.
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A phosphatidylinositol 3-kinase/Akt pathway promotes translocation of Mdm2 from the cytoplasm to the nucleus.

TL;DR: The demonstration that PI3-kinase/Akt signaling affects Mdm2 localization provides insight into how this pathway, which is inappropriately activated in many malignancies, affects the function of p53.
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