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• W4386797729 endingPage "122085" @default.
• W4386797729 startingPage "122085" @default.
• W4386797729 abstract "The SUMO family is a type of ubiquitin-like protein modification molecule. Its protein modification mechanism is similar to that of ubiquitination: both involve modifier-activating enzyme E1, conjugating enzyme E2 and substrate-specific ligase E3. However, polyubiquitination can lead to the degradation of substrate proteins, while poly-SUMOylation only leads to the degradation of substrate proteins through the proteasome pathway after being recognized by ubiquitin as a signal factor. There are currently five reported subtypes in the SUMO family, namely SUMO1-5. As a reversible dynamic modification, intracellular sentrin/SUMO-specific proteases (SENPs) mainly regulate the reverse reaction pathway of SUMOylation. The SUMOylation modification system affects the localization, activation and turnover of proteins in cells and participates in regulating most nuclear and extranuclear molecular reactions. Abnormal expression of proteins related to the SUMOylation pathway is commonly observed in tumors, indicating that this pathway is closely related to tumor occurrence, metastasis and invasion. This review mainly discusses the composition of members in the protein family related to SUMOylation pathways, mutual connections between SUMOylation and other post-translational modifications on proteins as well as therapeutic drugs developed based on these pathways." @default.
• W4386797729 created "2023-09-17" @default.
• W4386797729 creator A5013615744 @default.
• W4386797729 creator A5014343394 @default.
• W4386797729 date "2023-11-01" @default.
• W4386797729 modified "2023-10-11" @default.
• W4386797729 title "SUMOylation and DeSUMOylation: Prospective therapeutic targets in cancer" @default.
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