ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor (Q24306428)

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Ning Kon

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Muyang Li

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Wenzhu Zhang

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Jun Qin

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Wei Gu

Cocompartmentalization of p53 and Mdm2 is a major determinant for Mdm2-mediated degradation of p53.

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language of work or name

English

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publication date

1 July 2005

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published in

Cell

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volume

121

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issue

7

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page(s)

1071-83

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cites work

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Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53

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The Ink4a tumor suppressor gene product, p19Arf, interacts with MDM2 and neutralizes MDM2's inhibition of p53

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ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways

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p53- and Mdm2-Independent Repression of NF-κB Transactivation by the ARF Tumor Suppressor

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Mdm2 promotes the rapid degradation of p53

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Nucleolar Arf sequesters Mdm2 and activates p53

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Mdm2 association with p53 targets its ubiquitination

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An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo

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Requirement for p53 and p21 to sustain G2 arrest after DNA damage

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ARF function does not require p53 stabilization or Mdm2 relocalization

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ARF impedes NPM/B23 shuttling in an Mdm2-sensitive tumor suppressor pathway

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Physical and functional interactions of the Arf tumor suppressor protein with nucleophosmin/B23

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Nucleophosmin (B23) targets ARF to nucleoli and inhibits its function

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Mechanisms underlying ubiquitination

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Regulation of Membrane Protein Transport by Ubiquitin and Ubiquitin-Binding Proteins

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p19Arf suppresses growth, progression, and metastasis of Hras-driven carcinomas through p53-dependent and -independent pathways

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