Journal
FRONTIERS IN ONCOLOGY
Volume 11, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fonc.2021.679445
Keywords
MYC; protein stability; ubiquitination; deubiquitination; ubiquitin ligase; deubiquitinating enzyme; SUMOylation; SUMO-specific protease
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Funding
- NIH [R01 CA186241, R01 GM130604, U54 CA209988, U01 CA224012, R01 CA196228]
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Ubiquitination and SUMOylation are crucial mechanisms regulating the stability and activity of MYC protein, playing key roles in cancer and thereby serving as potential therapeutic targets.
Deregulated MYC overexpression and activation contributes to tumor growth and progression. Given the short half-life and unstable nature of the MYC protein, it is not surprising that the oncoprotein is highly regulated via diverse posttranslational mechanisms. Among them, ubiquitination dynamically controls the levels and activity of MYC during normal cell growth and homeostasis, whereas the disturbance of the ubiquitination/deubiquitination balance enables unwanted MYC stabilization and activation. In addition, MYC is also regulated by SUMOylation which crosstalks with the ubiquitination pathway and controls MYC protein stability and activity. In this mini-review, we will summarize current updates regarding MYC ubiquitination and provide perspectives about these MYC regulators as potential therapeutic targets in cancer.
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