Recent progress in the investigation of ubiquitination aberrance in osteosarcoma / 中华骨科杂志
Chinese Journal of Orthopaedics
;
(12): 1337-1348, 2018.
Artigo
em Chinês
| WPRIM
| ID: wpr-708660
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.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Idioma:
Chinês
Revista:
Chinese Journal of Orthopaedics
Ano de publicação:
2018
Tipo de documento:
Artigo
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