We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
The Next Frontier: Translational Development of Ubiquitination, SUMOylation, and NEDDylation in Cancer.
- Authors
Pellegrino, Nicole E.; Guven, Arcan; Gray, Kayleigh; Shah, Punit; Kasture, Gargi; Nastke, Maria-Dorothea; Thakurta, Anjan; Gesta, Stephane; Vishnudas, Vivek K.; Narain, Niven R.; Kiebish, Michael A.
- 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.
- Subjects
UBIQUITINATION; POST-translational modification; METABOLIC regulation; AMINO acid residues; PROTEIN structure
- Publication
International Journal of Molecular Sciences, 2022, Vol 23, Issue 7, p3480
- ISSN
1661-6596
- Publication type
Article
- DOI
10.3390/ijms23073480