Decoding Ubiquitination: Impact on Tumor Suppressor Protein Degradation and Cancer Progression

Research in the field of ubiquitination has unveiled it as a fundamental post-translational modification mechanism that meticulously directs protein fate within cells. Ubiquitination, a complex process involving a cascade of enzymatic reactions, is critically modulated by ubiquitinases. These enzymes facilitate the covalent binding of ubiquitin to specific lysine residues on target proteins. This modification serves as a dynamic regulatory cue, influencing the stability, location, activity, and interactions of the modified protein. Within cell biology, ubiquitination acts as an essential regulator, overseeing processes such as cell cycle dynamics, DNA repair pathways, and apoptosis. Significantly, tumor suppressor proteins—which are pivotal for cellular equilibrium—are frequently subject to ubiquitination. This modification has divergent effects; it may lead to their degradation, dampening their tumor-suppressive functions, or alternatively, activate them to counteract cell proliferation and prevent oncogenesis. Hence, an in-depth exploration of ubiquitination pathways that influence tumor suppressor proteins is crucial to understanding cancer progression and developing personalized therapeutics that restore cellular balance.

This Research Topic aims to elucidate the intricate relationship between ubiquitination regulation of tumor suppressor proteins and cancer progression. It intends to identify the key enzymes, such as E3 ligases and deubiquitinases (DUBs), involved in ubiquitination regulation. Examining their roles in regulating the stability and functionality of tumor suppressor proteins, along with understanding upstream and downstream regulatory mechanisms, is essential. Furthermore, the research aims to evaluate the therapeutic potential of intervening in these regulatory pathways to restore tumor suppressor functions and inhibit cancer advancement. Developing anti-cancer drugs targeting ubiquitination and validating their efficacy is also a primary objective.

To gather further insights into the ubiquitination regulation of tumor suppressor proteins and their effect on cancer progression, we welcome articles addressing, but not limited to, the following themes:

• Identification and analysis of key enzymes in tumor suppressor ubiquitination pathways.
• Examination of upstream and downstream regulatory mechanisms affecting tumor suppressors.
• Evaluation of the therapeutic effects of modulating ubiquitination pathways on cancer suppression.
• Development and validation of drugs targeting ubiquitination-related enzymatic processes.
• Utilization of bioinformatics and experimental approaches to model and validate regulatory networks in cancer.


Please note: Manuscripts consisting solely of bioinformatics, computational analysis, or predictions of public databases which are not accompanied by validation (independent clinical or patient cohort, or biological validation in vitro or in vivo, which are not based on public databases) are not suitable for publication in this journ

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This Research Topic accepts the following article types, unless otherwise specified in the Research Topic description:

• Brief Research Report
• Case Report
• Clinical Trial
• Editorial
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• General Commentary
• Hypothesis and Theory
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Article types

This Research Topic accepts the following article types, unless otherwise specified in the Research Topic description:

• Brief Research Report
• Case Report
• Clinical Trial
• Editorial
• FAIR² Data
• General Commentary
• Hypothesis and Theory
• Methods
• Mini Review
• Opinion
• Original Research
• Perspective
• Review
• Systematic Review
• Technology and Code

Keywords: Ubiquitination, Ubiquitin Proteasomal System(UPS), Tumour Suppressor Proteins, Cancer Progression, Molecular Mechanisms

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