Looking Back and Ahead: Emerging Concepts in Ubiquitin and UBLs
A special issue of Biomolecules (ISSN 2218-273X).
Deadline for manuscript submissions: closed (15 February 2021) | Viewed by 27200
Special Issue Editors
Interests: ubiquitin-like molecules; cell growth regulation
Interests: ubiquitin-like molecules; cell growth regulation
Special Issue Information
Dear Colleagues,
Post-translational modification by ubiquitin and ubiquitin-like (UBL) modifiers plays a crucial role in cellular signal transduction, by controlling function, localization, and interactions of a large number of proteins. Both the conjugation of ubiquitin and UBLs occurs through the sequential action of three enzymes, called activating enzyme (E1), conjugating enzyme (E2), and ligase (E3). It has been ascertained that this machinery generates different profiles of protein modification, each having a specific functional outcome. Indeed, while ubiquitin chains were initially described as a signal for proteasomal degradation, nondegradative ubiquitination has proved to be a key modification in endocytosis, histone modifications, transcriptional regulation, and kinase signaling. Likewise, the conjugation of UBLs like NEDD8 and SUMO has proven to be a key node in distinct regulatory networks, such as the regulation of the immune system, cell cycle control, and cell death. Notably, SUMO and NEDD8 also form chains; moreover, SUMO chains can be targeted for ubiquitination, and ubiquitin can be subjected to neddylation and sumoylation. The functional role of these covalent modifications primarily depends on their recognition by receptors containing binding domains that dictate the formation of noncovalent protein complexes driving the specificity of the signal transduction process. Dysfunction within these mechanisms leads to severe pathological conditions, among them neurodegenerative diseases and cancers.
The central role of ubiquitin and UBLs in such diverse cellular processes makes them attractive targets for selective drug discovery. This issue aims to enlighten researchers on progress regarding the new functions and regulatory roles of ubiquitin and UBLs.
Prof. Dmitris Xirodimas
Dr. Elena Santonico
Guest Editors
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Keywords
- ubiquitin
- ubiquitin-like (UBL)
- post-translational modification (PTM)
- protein degradation
- E1
- E2
- E3