Dear Colleagues,
The ubiquitination pathway controls a diverse array of cellular and biological processes to ensure proper functioning of proteins in cells. These processes include cell cycle progression, protein and organelle turnover, protein trafficking, endocytosis and DNA repair. It is a tightly regulated process achieved through the synchronized action of three enzymes - E1 ubiquitin activating, E2 ubiquitin conjugating and E3 ligases. Ubiquitination is a process whereby ubiquitin is covalently attached to a protein and influences its movement within the cell. It is also involved in the synthesis of new proteins and the destruction of defective proteins. Thus, the addition and removal of ubiquitin is crucial in determining a protein’s fate in the cell. Dysregulation of components within the ubiquitin pathway has been extensively linked to various diseases such as cancer, neurodegenerative diseases, cardiovascular diseases, and hypertension. However, progress in targeting the ubiquitin pathway has been slow and this delay has been attributed to the following reasons: (i) most components of the ubiquitin system do not possess a well-defined catalytic pocket that would allow the binding of small molecule inhibitors, (ii) the ubiquitination process relies on dynamic rearrangement of multiple protein–protein interactions that are difficult to disrupt with small molecule inhibitors, and (iii) components of the ubiquitin system possess both oncogenic and tumour suppressor properties arising from the complexity of their regulatory cellular processes. Despite these challenges, abnormalities within the ubiquitin system are still attractive targets for drug discovery and many pharmacologically active compounds that affect ubiquitination have been identified in preclinical studies. This highlights current efforts to unlock the potential for targeting of this pathway in various diseases. In this Special Issue of Frontiers in Biosciences, we invite authors to contribute original research articles, perspective or reviews on recent insights or progress regarding the mechanism, function and pharmacological dissection of the ubiquitination pathway in both non-disease and disease conditions. We look forward to your contribution.
Dr. Azhar Ali
Guest Editor
Manuscripts should be submitted via our online editorial system at https://imr.propub.com by registering and logging in to this website. Once you are registered, click here to start your submission. Manuscripts can be submitted now or up until the deadline. All papers will go through peer-review process. Accepted papers will be published in the journal (as soon as accepted) and meanwhile listed together on the special issue website. Research articles, reviews as well as short communications are preferred. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office to announce on this website.
Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts will be thoroughly refereed through a double-blind peer-review process. Please visit the Instruction for Authors page before submitting a manuscript. The Article Processing Charge (APC) in this open access journal is 2500 USD. Submitted manuscripts should be well formatted in good English.
- Open Access Original ResearchThe Deubiquitinating Enzyme USP4 Functions as an Oncoprotein in Gastric Cancer and Mediates NF-κB Signaling by Regulating PRL-3 ExpressionYuanyuan Tao, Wendao YouFront. Biosci. (Landmark Ed) 2022, 27(10), 286; https://doi.org/10.31083/j.fbl2710286(This article belongs to the Special Issue Ubiquitin Signaling in Health and Disease)44Downloads173Views