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[The role of different E3 ubiquitin ligases in regulation of the P53 tumor suppressor protein].
- Source :
-
Tsitologiia [Tsitologiia] 2013; Vol. 55 (10), pp. 673-87. - Publication Year :
- 2013
-
Abstract
- Ubiquitin-dependent proteasomal degradation is one of the major pathways of non-lysosomal protein degradation in the cell. The ubiquitination process involves several enzymatic reactions and includes the following enzymes: E1--activating, E2--conjugating, and the third--E3--ligating enzymes. E3 ligases determine the specificity of ubiquitination reaction, i. e. what target protein will be subjected to the covalent modification by ubiquitins. The p53b tumor suppressor protein is one of the most intensively studied over the past several decades. Regulation of its activity is a complex and multi-level process that involves many factors. Ubiquitination is one of the major post-translational modifications of p53, and plays a fundamental role in the control of p53 function, its amount, activity and subcellular localization. This review is focused on p53-specific E3 ubiquitin ligases that are potential targets for cancer therapy using small molecule inhibitors.
- Subjects :
- Animals
Antineoplastic Agents chemistry
Antineoplastic Agents therapeutic use
Enzyme Inhibitors chemistry
Enzyme Inhibitors therapeutic use
Humans
Isoenzymes genetics
Isoenzymes metabolism
Neoplasms drug therapy
Neoplasms genetics
Neoplasms pathology
Proteasome Endopeptidase Complex genetics
Proteasome Endopeptidase Complex metabolism
Proteolysis
Tumor Suppressor Protein p53 genetics
Ubiquitin genetics
Ubiquitin metabolism
Ubiquitin-Protein Ligases antagonists & inhibitors
Ubiquitin-Protein Ligases genetics
Ubiquitination
Gene Expression Regulation
Neoplasms enzymology
Protein Processing, Post-Translational
Tumor Suppressor Protein p53 metabolism
Ubiquitin-Protein Ligases metabolism
Subjects
Details
- Language :
- Russian
- ISSN :
- 0041-3771
- Volume :
- 55
- Issue :
- 10
- Database :
- MEDLINE
- Journal :
- Tsitologiia
- Publication Type :
- Academic Journal
- Accession number :
- 25509121