Cited by 818Cancer-related Molecular PathwaysDNA Repair MechanismsProtein Kinase Regulation and GTPase Signaling

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DNA damage induces phosphorylation of the amino terminus of p53

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Siliciano, Janet D., Canman, Christine E., Taya, Yoichi, Sakaguchi, Kazuyasu, Appella, Ettore, Kastan, Michael B.·1997·Genes & Development

DOI 10.1101/gad.11.24.3471PMC PMC316806

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Abstract

Data are presented demonstrating that DNA damage leads to specific post-translational modifications of p53 protein. Using two-dimensional peptide mapping of in vivo radiolabeled p53 tryptic phosphopeptides, recombinant truncated p53 protein, and synthetic p53 tryptic peptides, a unique p53 phosphopeptide was identified after exposure of ML-1 cells to ionizing irradiation. This peptide represents the first 24 amino acids of p53 and contains three phosphorylated serine residues. A specific p53 phosphopeptide antibody identified serine-15 as one of the two serines in p53 that becomes phosphorylated following DNA damage induced by either ionizing irradiation (IR) or ultraviolet (UV) irradiation in multiple cell types. IR-induced phosphorylation of p53 does not affect the kinetics of p53 binding to or dissociating from DNA as assessed by electrophoretic mobility-shift assays. However, p53 phosphorylation induced by DNA damage correlates with enhanced transcription of downstream p53 target genes. Low levels of phosphoserine-15 p53 are detectable within 6 hr after IR in AT cells, whereas lymphoblasts from normal individuals exhibit this modification within 1 hr. In contrast, phosphorylation of p53 on serine-15 is similar in normal and AT cells after UV irradiation. Our results indicate that p53 is phosphorylated in response to DNA damage, that this de novo phosphorylation may be involved in the subsequent induction and activation of p53, and that although ATM affects the kinetics of p53 phosphorylation after IR, it is not absolutely required for phosphorylation of p53 on serine-15.

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Background
JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
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True
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Authors: Siliciano, J. D., Canman, C. E., Taya, Y., Sakaguchi, K., Appella, E., & Kastan, M. B.
Affiliations: National Institutes of Health (US)
ORCID: Siliciano, Janet D.
Canman, Christine E.
Sakaguchi, Kazuyasu
Appella, Ettore
Kastan, Michael B.
Venue: Genes & Development
Publisher: Cold Spring Harbor Laboratory
Published: 1997-12-15
Volume: 11
Issue: 24
Pages: 3471-3481
ISSN: 0890-9369 (ISSN-L)
1549-5477
DOI: 10.1101/gad.11.24.3471
PMC: PMC316806
OpenAlex: W2149013144
Cited by: 818
References: 71
Citations by year: 2026: 4 · 2025: 3 · 2024: 5 · 2023: 7 · 2022: 10 · 2021: 10 · 2020: 12 · 2019: 14 · 2018: 12 · 2017: 18 · 2016: 22 · 2015: 17 · 2014: 24 · 2013: 21 · 2012: 27
Type: posted content
Language: en
Open access: bronze
doi.org
Locations: Genes & Development (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
HighWire Press Open Archive (submittedVersion)
Funders: American Society of Hematology
National Institutes of Health (ES05777)
National Cancer Institute (CA71387, R01CA071387)
National Institute of Environmental Health Sciences (R01ES005777, R37ES005777, ES05777)
Topics: Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords: p53, DNA damage response, ionizing radiation, UV irradiation, post-translational modification, ATM kinase, lymphoblasts
MeSH terms: Ataxia Telangiectasia, Binding Sites, Cells, Cultured, DNA, DNA Damage, Electrophoresis, Humans, Lymphocytes, Nuclear Proteins, Peptide Fragments, Phosphorylation, Protein Processing, Post-Translational, Proto-Oncogene Proteins, Serine, Ultraviolet Rays, Signal Transduction, Tumor Suppressor Protein p53, Cyclins, Cyclin-Dependent Kinase Inhibitor p21, Proto-Oncogene Proteins c-mdm2

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DNA damage induces phosphorylation of the amino terminus of p53

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