DNA damage induces phosphorylation of the amino terminus of p53.
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Summary
The 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 p52 phosphorylate after IR, it is not absolutely required for phosphorylations of p 53 on serine-15.
- Type
- article
- Published
- 1997-12-15
- Cited by
- 906
- References
- 54
- Access
- Open access
- OpenAlex
- https://openalex.org/W2149013144
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:19625261
Keywords
Phosphoserine, Phosphorylation, Phosphopeptide, Serine, DNA damage
References
- Human p53 is phosphorylated by p60-cdc2 and cyclin B-cdc2.
- The consensus motif for phosphorylation by cyclin D1‐Cdk4 is different from that for phosphorylation by cyclin A/E‐Cdk2.
- Mutation of the serine 15 phosphorylation site of human p53 reduces the ability of p53 to inhibit cell cycle progression.
- Sequence‐specific DNA binding by p53: identification of target sites and lack of binding to p53 ‐ MDM2 complexes.
- Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates.
- Serine phosphorylation in the NH2 terminus of p53 facilitates transactivation.
- DNA-dependent protein kinase is not required for accumulation of p53 or cell cycle arrest after DNA damage.
- p53-dependent cell cycle arrests are preserved in DNA-activated protein kinase-deficient mouse fibroblasts.
- Phosphorylation of the tumor suppressor protein p53 by mitogen-activated protein kinases.
- Mapping of the p53 and mdm-2 interaction domains.
- In vivo ubiquitination and proteasome-mediated degradation of p53(1).
- Participation of p53 protein in the cellular response to DNA damage.
- Dual roles of ATM in the cellular response to radiation and in cell growth control.
- p53 Is Phosphorylated in Vitro and in Vivo by an Ultraviolet Radiation-induced Protein Kinase Characteristic of the c-Jun Kinase, JNK1 (*)
- Increased and altered DNA binding of human p53 by S and G2/M but not Gl cyclin-dependent kinases
- p53 in growth control and neoplasia.
- DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2.
- ATM-related genes: what do they tell us about functions of the human gene?
- JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain.
- A mammalian cell cycle checkpoint pathway utilizing p53 and GADD45 is defective in ataxia-telangiectasia.
Cited by
- Critical role for Ser20 of human p53 in the negative regulation of p53 by Mdm2
- Regulation of p53 stability
- The catalytic subunit of DNA-dependent protein kinase selectively regulates p53-dependent apoptosis but not cell-cycle arrest.
- The onset of p53-dependent DNA repair or apoptosis is determined by the level of accumulated damaged DNA.
- Mdm-2 binding and TAFII31 recruitment is regulated by hydrogen bond disruption between the p53 residues Thr18 and Asp21
- Melanoma cells express elevated levels of phosphorylated histone H2AX foci.
- Physical and Functional Interaction between Ribosomal Protein L11 and the Tumor Suppressor ARF*
- Another fork in the road—life or death decisions by the tumour suppressor p53
- Clinical Significance of the Wild Type p53‐Induced Phosphatase 1 Expression in Invasive Breast Cancer
- Integration of the PRB and P53 Cell Cycle Control Pathways
- Protective Effects of Milk Phospholipids against UV-induced DNA Damage in Human Skin Cells
- Analyzing the G2/M checkpoint.
- Molekularer Mechanismus der Stickstoffmonoxid-vermittelten Akkumulation des Tumorsuppressors p53
- Doctorate Program in Molecular Oncology and Endocrinology
- Cell Cycle Control
- GEMC1, a novel factor required for chromosomal DNA replication
- Biochemical characterization of Aprataxin, the protein deficient in Ataxia with Oculomotor Apraxia type 1
- Regulation of p53 downstream genes.
- Involvement of p53 in the repair of DNA double strand breaks: Multifaceted roles of p53 in homologous recombination repair (HRR) and non-homologous end joining (NHEJ)
- Silencing, Heterochromatin and DNA Double Strand Break Repair
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