Inhibition of protein SUMOylation by natural quinones
| Autor: | Yasuhiro Igarashi, Mohammad Tariq, Isao Fukuda, Hisato Saitoh, Minoru Yoshida, Mikako Hirohama, Akihiro Ito |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Protein sumoylation DNA repair Drug Evaluation Preclinical SUMO protein SUMO enzymes 01 natural sciences Inhibitory Concentration 50 03 medical and health sciences Ubiquitin Transcription (biology) Drug Discovery Enzyme Inhibitors Pharmacology chemistry.chemical_classification Biological Products Molecular Structure biology 010405 organic chemistry Quinones DNA replication Sumoylation 0104 chemical sciences 030104 developmental biology Enzyme chemistry Biochemistry biology.protein |
| Zdroj: | The Journal of Antibiotics. 69:776-779 |
| ISSN: | 1881-1469 0021-8820 |
| DOI: | 10.1038/ja.2016.23 |
| Popis: | Conjugation of small ubiquitin-related modifier (SUMO) to target proteins (SUMOylation) is a posttranslational modification that regulates a wide range of biological processes, including transcription, intracellular transport, DNA repair, DNA replication and cell signaling.1 SUMOylation is catalyzed by a multi-step enzymatic cascade that resembles ubiquitination: the process involves an E1-activating enzyme (a heterodimer consisting of Aos1 and Uba2), an E2-conjugating enzyme (Ubc9) and various E3 ligases.1 E3s catalyze SUMO conjugation to target proteins and may contribute to substrate specificity. SUMO is subsequently cleaved from target proteins by SUMO-specific isopeptidases. Because SUMO modifications have been implicated in a variety of disorders such as cancers2 and neurodegenerative diseases,3 the enzymes involved in SUMOylation are promising targets for therapeutic agents. |
| Databáze: | OpenAIRE |
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