Essential Roles of E3 Ubiquitin Ligases in p53 Regulation
AbstractThe ubiquitination pathway and proteasomal degradation machinery dominantly regulate p53 tumor suppressor protein stability, localization, and functions in both normal and cancerous cells. Selective E3 ubiquitin ligases dominantly regulate protein levels and activities of p53 in a large range of physiological conditions and in response to cellular changes induced by exogenous and endogenous stresses. The regulation of p53’s functions by E3 ubiquitin ligases is a complex process that can lead to positive or negative regulation of p53 protein in a context- and cell type-dependent manner. Accessory proteins bind and modulate E3 ubiquitin ligases, adding yet another layer of regulatory control for p53 and its downstream functions. This review provides a comprehensive understanding of p53 regulation by selective E3 ubiquitin ligases and their potential to be considered as a new class of biomarkers and therapeutic targets in diverse types of cancers. View Full-Text
Scifeed alert for new publicationsNever miss any articles matching your research from any publisher
- Get alerts for new papers matching your research
- Find out the new papers from selected authors
- Updated daily for 49'000+ journals and 6000+ publishers
- Define your Scifeed now
Sane, S.; Rezvani, K. Essential Roles of E3 Ubiquitin Ligases in p53 Regulation. Int. J. Mol. Sci. 2017, 18, 442.
Sane S, Rezvani K. Essential Roles of E3 Ubiquitin Ligases in p53 Regulation. International Journal of Molecular Sciences. 2017; 18(2):442.Chicago/Turabian Style
Sane, Sanam; Rezvani, Khosrow. 2017. "Essential Roles of E3 Ubiquitin Ligases in p53 Regulation." Int. J. Mol. Sci. 18, no. 2: 442.
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.