Multiple Lysine Mutations in the C-Terminal Domain of p53 Interfere with MDM2-Dependent Protein Degradation and Ubiquitination
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Summary
It is suggested that mutations in the putative acetylation sites of the p53 C-terminal domain interfere with ubiquitination, thereby regulating p53 degradation.
- Type
- article
- Published
- 2000-12-01
- Cited by
- 224
- References
- 37
- Access
- Open access
- OpenAlex
- https://openalex.org/W2119363024
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:20517409
Keywords
Biology, Lysine, Transactivation, Nuclear export signal, Ubiquitin
References
- Human TAFII31 protein is a transcriptional coactivator of the p53 protein.
- Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
- Multisite phosphorylation and the integration of stress signals at p53.
- Cell type‐specific inhibition of p53‐mediated apoptosis by mdm2.
- In vivo ubiquitination and proteasome-mediated degradation of p53(1).
- Nuclear Export Is Required for Degradation of Endogenous p53 by MDM2 and Human Papillomavirus E6
- A transcriptionally active DNA-binding site for human p53 protein complexes
- Oncoprotein MDM2 conceals the activation domain of tumour suppressor p53
- DNA damage activates p53 through a phosphorylation-acetylation cascade.
- DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2.
- A mammalian cell cycle checkpoint pathway utilizing p53 and GADD45 is defective in ataxia-telangiectasia.
- Regulation of the specific DNA binding function of p53.
- Regulation of the cryptic sequence-specific DNA-binding function of p53 by protein kinases.
- WAF1, a potential mediator of p53 tumor suppression.
- Several hydrophobic amino acids in the p53 amino-terminal domain are required for transcriptional activation, binding to mdm-2 and the adenovirus 5 E1B 55-kD protein.
- Association of p19ARF with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
- Tumor suppressor p53 is a direct transcriptional activator of the human bax gene.
- Regulation of p53 stability by Mdm2
- Oligomerization Is Required for p53 to be Efficiently Ubiquitinated by MDM2*
- p53 transcriptional activation mediated by coactivators TAFII40 and TAFII60.
Cited by
- Regulation of p53 function.
- Protein phosphatase Mg2+/Mn2+ dependent 1F promotes smoking-induced breast cancer by inactivating phosphorylated-p53-induced signals
- Ubiquitin Family Members in the Regulation of the Tumor Suppressor p53.
- The subcellular distribution of the p53 tumour suppressor, and organismal ageing.
- SRD5A2 gene expression inhibits cell migration and invasion in prostate cancer cell line via F-actin reorganization
- Novel DNA damage induced pathways to cancer : the role of PCAF histone acetyltransferase
- The regulation of preadipocyte differentiation by glucocorticoids
- NIAM, a novel activator of p53 and potential tumor suppressor
- Protein methylation: a new regulator of the p53 tumor suppressor
- p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity.
- Contribution of the DNA binding domain of p53 to regulation of its stability
- Multiple modes of Mdmx regulation affect p53 activation
- Investigations into the expression of sirtuins in breast cancer: in vivo and in vitro studies
- Regulation of insulin-like growth factor-1 receptor expression and signaling
- Funktionelle Interaktionen zwischen Wildtyp-p53, Rad51 und Poly-ADP-Phosphoribosyl-Transferase bei der Kontrolle von DNA-Rekombinationsprozessen
- To reactivate or not to reactivate : Control of KSHV lytic replication is essential for apoptosis in response to p53 restoration
- Selectivity of E2-E3 interactions in the human ubiquitin system
- Mdm2: A regulator of cell growth and death.
- Induction of PIG3 and NOXA through acetylation of p53 at 320 and 373 lysine residues as a mechanism for apoptotic cell death by histone deacetylase inhibitors.
- Large scale analysis of the mutational landscape in β-glucuronidase: A major player of mucopolysaccharidosis type VII.
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