Abstract

Cells perform several post-translational changes in various proteins prior to allow their participation in various intracellular metabolic mechanisms. Ubiquitylation is also a post-translational process for different cellular proteins after which modified proteins contribute their physiological functions in distinct cellular processes. E3 ubiquitin ligases are important components of ubiquitin proteasome system (UPS), which specifically recognize critical substrate proteins (abnormal, over-accumulated & old) for their intracellular elimination. Loss of cell cycle regulation is one of the chief possible causes of deregulated cellular proliferation and cancer progression. How different E3 ubiquitin ligases play essential roles in cell-cycle regulation is still one of the unsolved fundamental questions and potentially stands for the development of early diagnostic methods, which can generate new molecular strategies to treat cancer. In this chapter, our main focus is to understand the functions of E3 Ubiquitin Ligases as setting potential biomarker or targets in various cancers and linked with regulatory roles of cell-cycle transitions. The chief objective of this current chapter is to understand the critical requirement of new biomarkers, which can early indicate improper cellular proliferation and cancer progression due to the complex defects in various signal transduction mechanisms linked with the promotion and progress of each phase of the cell cycle. A better understanding of E3 ubiquitin ligases may result in new insights and therapeutic strategies for the treatment and suppression of the development of cancer.

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