Cited by 899Cancer-related Molecular PathwaysHeat shock proteins researchChromatin Remodeling and Cancer

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Functional and physical interactions of the ARF tumor suppressor with p53 and Mdm2

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Kamijo, Takehiko, Weber, Jason D., Zambetti, Gerard, Zindy, Frederique, Roussel, Martine F., Sherr, Charles J.·1998·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.95.14.8292PMC PMC20969

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Abstract

The INK4a-ARF locus encodes two proteins, p16(INK4a) and p19(ARF), that restrain cell growth by affecting the functions of the retinoblastoma protein and p53, respectively. Disruption of this locus by deletions or point mutations is a common event in human cancer, perhaps second only to the loss of p53. Using insect cells infected with baculovirus vectors and NIH 3T3 fibroblasts infected with ARF retrovirus, we determined that mouse p19(ARF) can interact directly with p53, as well as with the p53 regulator mdm2. ARF can bind p53-DNA complexes, and it depends upon functional p53 to transcriptionally induce mdm2 and the cyclin-dependent kinase inhibitor p21(Cip1), and to arrest cell proliferation. Binding of p19(ARF) to p53 requires the ARF N-terminal domain (amino acids 1-62) that is necessary and sufficient to induce cell cycle arrest. Overexpression of p19(ARF) in wild type or ARF-null mouse embryo fibroblasts increases the half-life of p53 from 15 to approximately 75 min, correlating with an increased p53-dependent transcriptional response and growth arrest. Surprisingly, when overexpressed at supra-physiologic levels after introduction into ARF-null NIH 3T3 cells or mouse embryo fibroblasts, the p53 protein is handicapped in inducing this checkpoint response. In this setting, reintroduction of p19(ARF) restores p53's ability to induce p21(Cip1) and mdm2, implying that, in addition to stabilizing p53, ARF modulates p53-dependent function through an additional mechanism.

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Authors: Kamijo, T., Weber, J. D., Zambetti, G., Zindy, F., Roussel, M. F., & Sherr, C. J.
Affiliations: St. Jude Children's Research Hospital (US)
Howard Hughes Medical Institute and Departments of Tumor Cell Biology and Biochemistry, St. Jude Children’s Research Hospital, 332 North Lauderdale, Memphis, TN 38105
Corresponding author: Sherr, Charles J.
ORCID: Kamijo, Takehiko
Weber, Jason D.
Zambetti, Gerard
Roussel, Martine F.
Sherr, Charles J.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1998-07-07
Volume: 95
Issue: 14
Pages: 8292-8297
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.95.14.8292
PMC: PMC20969
OpenAlex: W2141529421
Cited by: 899
References: 61
Citations by year: 2026: 5 · 2025: 5 · 2024: 2 · 2023: 10 · 2022: 11 · 2021: 15 · 2020: 10 · 2019: 10 · 2018: 12 · 2017: 14 · 2016: 26 · 2015: 21 · 2014: 33 · 2013: 28 · 2012: 34
FWCI: 31.09
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: St. Jude Children's Research Hospital (CA21765)
American Lebanese Syrian Associated Charities (CA 21765)
National Institutes of Health (CA21765))
National Cancer Institute (R01CA063230, CA-71907, CA-63230, CA21765, P30CA021765, P01CA071907)
Topics: Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
Keywords: p19ARF, p53, MDM2, INK4a/ARF locus, p16INK4a, protein-protein interaction, p53 stabilization, p21 Cip1, cell cycle arrest, p53-dependent transcription, tumor suppressor, p53 DNA binding, N-terminal domain
MeSH terms: Animals, Humans, Neoplasm Proteins, Nuclear Proteins, Proteins, Proto-Oncogene Proteins, Retroviridae, Transfection, Gene Expression Regulation, Neoplastic, Genes, Tumor Suppressor, Tumor Suppressor Protein p53, 3T3 Cells, Tumor Suppressor Protein p14ARF, Mice, Proto-Oncogene Proteins c-mdm2

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Functional and physical interactions of the ARF tumor suppressor with p53 and Mdm2

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