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 endocytosis, 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.
Published Version
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