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Updated: Sep 27, 2025

SUMO-Binding Entities SUBEs as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer
Published on: November 1, 2019
The Next Frontier: Translational Development of Ubiquitination, SUMOylation, and NEDDylation in Cancer
Nicole E Pellegrino1, Arcan Guven1, Kayleigh Gray1
1BERG, 500 Old Connecticut Path, Framingham, MA 01701, USA.
Abstract:
Post-translational modifications of proteins ensure optimized cellular processes, including proteostasis, regulated signaling, cell survival, and stress adaptation to maintain a balanced homeostatic state. Abnormal post-translational modifications are associated with cellular dysfunction and the occurrence of life-threatening diseases, such as cancer and neurodegenerative diseases. Therefore, some of the frequently seen protein modifications have been used as disease markers, while others are targeted for developing specific therapies. The ubiquitin and ubiquitin-like post-translational modifiers, namely, small ubiquitin-like modifier (SUMO) and neuronal precursor cell-expressed developmentally down-regulated protein 8 (NEDD8), share several features, such as protein structures, enzymatic cascades mediating the conjugation process, and targeted amino acid residues. Alterations in the regulatory mechanisms lead to aberrations in biological processes during tumorigenesis, including the regulation of tumor metabolism, immunological modulation of the tumor microenvironment, and cancer stem cell stemness, besides many more. Novel insights into ubiquitin and ubiquitin-like pathways involved in cancer biology reveal a potential interplay between ubiquitination, SUMOylation, and NEDDylation. This review outlines the current understandings of the regulatory mechanisms and assay capabilities of ubiquitination, SUMOylation, and NEDDylation. It will further highlight the role of ubiquitination, SUMOylation, and NEDDylation in tumorigenesis.
Insights
Post-translational modifications like ubiquitination, SUMOylation, and NEDDylation regulate cellular processes. Aberrations in these pathways are linked to cancer, highlighting their therapeutic potential.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Post-translational modifications (PTMs) are crucial for cellular functions, including proteostasis and stress adaptation.
- Dysregulated PTMs are implicated in diseases like cancer and neurodegenerative disorders.
- Ubiquitin and ubiquitin-like modifiers (SUMOylation, NEDDylation) share structural and enzymatic similarities.
Purpose of the Study:
- To review regulatory mechanisms and assay capabilities of ubiquitination, SUMOylation, and NEDDylation.
- To highlight the interplay between these PTMs in cancer biology.
- To explore their roles in tumorigenesis.
Main Methods:
- Literature review of regulatory mechanisms.
- Analysis of assay capabilities for PTMs.
- Synthesis of current understanding of PTMs in cancer.
Main Results:
- Ubiquitination, SUMOylation, and NEDDylation pathways share conserved features.
- Aberrations in these pathways contribute to tumorigenesis.
- These PTMs influence tumor metabolism, immune microenvironment, and cancer stemness.
Conclusions:
- Understanding the interplay of ubiquitination, SUMOylation, and NEDDylation is vital for cancer research.
- These PTMs represent potential targets for cancer therapy.
- Further research into PTM regulatory mechanisms and assays is warranted.
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