Covalent and Non-covalent Functions of Ubiquitin and Ubiquitin-Like Molecules: Emerging Concepts

Dear Colleagues,

Protein degradation is at the heart of many cellular pathways, and the ubiquitin–proteasome system (UPS) is central to this process. Proteolysis is guided by the covalent attachment of ubiquitin to target proteins using E1 (activating), E2 (conjugating), and E3 (ligating) enzymes in a process known as ubiquitylation. This complex machinery generates different profiles of protein modification, each having a specific functional outcome. The significance of UPS is underscored by its involvement in various physiological processes and its implications in disease, making it a vital area of study in cell biology and medicine. The UPS ensures that redundant or damaged/misfolded proteins are rapidly degraded, preventing the potential toxic effects of their accumulation. It controls the level of key regulatory proteins, regulating cell cycle progression, signal transduction, and apoptosis. The UPS also supports the cellular response to stress conditions such as heat shock or oxidative stress. Finally, it regulates protein synthesis by influencing multiple steps of RNA (ribonucleic acid) metabolism. The tight interplay between the UPS and the protein homeostasis status of the cell is further enriched by parallel but distinct regulatory networks based on the conjugation of ubiquitin-like molecules (UBLs). These extend the regulatory capabilities of the ubiquitin–proteasome system by providing additional layers of control over protein function and stability. This Special Issue aims to enlighten researchers on the exciting progress regarding the new functions and regulatory roles of ubiquitin and UBLs, highlighting their importance in cellular biology and potential therapeutic applications.

Dr. Elena Santonico
Dr. Dmitris Xirodimas
Guest Editors

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