Ubiquitination and Deubiquitination in Oral Disease

Abstract

Oral health is an integral part of the general health and well-being of individuals. The presence of oral disease is potentially indicative of a number of systemic diseases and may contribute to their early diagnosis and treatment. The ubiquitin (Ub) system has been shown to play a role in cellular immune response, cellular development, and programmed cell death. Ubiquitination is a post-translational modification that occurs in eukaryotes. Its mechanism involves a number of factors, including Ub-activating enzymes, Ub-conjugating enzymes, and Ub protein ligases. Deubiquitinating enzymes, which are proteases that reversely modify proteins by removing Ub or Ub-like molecules or remodeling Ub chains on target proteins, have recently been regarded as crucial regulators of ubiquitination-mediated degradation and are known to significantly affect cellular pathways, a number of biological processes, DNA damage response, and DNA repair pathways. Research has increasingly shown evidence of the relationship between ubiquitination, deubiquitination, and oral disease. This review investigates recent progress in discoveries in diseased oral sites and discusses the roles of ubiquitination and deubiquitination in oral disease.

UBE2T promotes glioblastoma malignancy through ubiquitination‐mediated degradation of RPL6

“…Ubiquitination plays an important role in enzyme activity, protein stability, and interaction between proteins 4 . Disorders in the regulation of ubiquitination could lead to abnormal gene expression, which affects the tumorigenesis and development of tumors 5–7 . E3 ligase TRIM22 bound IκBα, a negative regulator of NF‐κB, accelerated its degradation by inducing K48‐linked polyubiquitination and promoted tumor growth and treatment resistance in GBM 8 .…”

“…4 Disorders in the regulation of ubiquitination could lead to abnormal gene expression, which affects the tumorigenesis and development of tumors. [5][6][7] E3 ligase TRIM22 bound IκBα, a negative regulator of NF-κB, accelerated its degradation by inducing K48-linked polyubiquitination and promoted tumor growth and treatment resistance in GBM. 8 The E3 ligase TRIM45 acts as a tumor suppressor in glioma.…”

USP44 accelerates the growth of T-cell acute lymphoblastic leukemia through interacting with WDR5 and repressing its ubiquitination

“…Ubiquitination, a form of post-translation modification, leads to protein degradation. The ubiquitination/deubiquitination system is critical in various physiological events by participating in intracellular signaling pathways 2 , 3 . Ubiquitin-specific protease 44 (USP44), a kind of deubiquitinase, is implicated in modulating innate immune responses 4 , spindle checkpoints and centrosome positioning 5 , stem cell differentiation 6 and DNA damage response 7 .…”