Recent progress in the investigation of ubiquitination aberrance in osteosarcoma
10.3760/cma.j.issn.0253-2352.2018.21.008
- VernacularTitle:蛋白泛素化修饰异常与骨肉瘤研究进展
- Author:
Jun ZHAO
1
;
Guolong LIU
;
Gang MA
;
Liren LIU
Author Information
1. 300060 天津医科大学肿瘤医院,国家肿瘤临床医学研究中心,骨与软组织肿瘤科
- From:
Chinese Journal of Orthopaedics
2018;38(21):1337-1348
- CountryChina
- Language:Chinese
-
Abstract:
Ubiquitination is one of the most important post-translational modification processes in eukaryotic cells,in which the ubiquitin molecules and/or ubiquitin chains are covalently transferred to the substrate after a series of enzymatic cascade reactions involving the activating (E1),conjugating (E2) and ligating (E3) enzymes.Coupling to the 26S proteasome complex to form the Ubiquitin-Proteasome System (UPS),ubiquitination plays an essential role in controlling protein stability,thereby maintaining the dynamic balance of the key cellular proteins.Besides,ubiquitination is also involved in a wide range of protein degradation-independent events,such as gene transcription and translation,signal transduction,DNA repair and endocytoais,exerting a key function in response to exogenous stimuli and the cellular homeostasis.Similar to kinases,components of the ubiquitination system are often dysregulated,leading to a variety of diseases,such as cancer.Recently,accumulating evidence has shown an increasing number of dysregulated ubiquitination processes in osteosarcoma (OS).Herein,this review briefly provides current perspectives on the aberrance of ubiquitination-associated factors and their roles in OS,providing novel insight into potential therapeutic targets of OS.
