About this Research Topic

Background

The ubiquitin–proteasome system (UPS) regulates the degradation of proteins involved in various cellular processes, making it crucial for maintaining cellular homeostasis. In cancer, dysregulation of UPS-mediated protein degradation contributes to tumor initiation, progression, and metastasis. E3 ubiquitin ligases, key components of the UPS, mark specific proteins for degradation by tagging them with ubiquitin molecules. The UPS impacts numerous pathways implicated in cancer biology, including cell cycle control, apoptosis, DNA damage response, and cellular signaling. Dysfunctional UPS activity can lead to aberrant protein accumulation, disrupting cellular processes essential for tumor suppression and promoting oncogenesis. This aberrant protein accumulation can be degraded via targeted protein degradation (TPD) using small molecules like PROTAC. Understanding the intricate signaling processes and TPD mechanisms mediated by the UPS in cancer is paramount for developing targeted therapies aimed at restoring proteostasis and halting tumor progression.

The goal of this journal issue is to shed light on the multifaceted nature of aberrant protein accumulation in cancer, driven by dysregulated ubiquitin–proteasome system (UPS) activity. We aim to elucidate the intricate mechanisms underlying UPS dysfunction and its profound implications for tumor initiation, progression, and metastasis. Research in this area encompasses a multidisciplinary approach, integrating insights from molecular biology, genetics, epigenetics, and cellular signaling to unravel the complexities of UPS-mediated protein degradation in cancer. By fostering collaboration across diverse fields, we seek to advance our understanding of cancer biology and explore innovative therapeutic strategies, such as TPD using small molecule degraders like PROTACs, to restore proteostasis and halt tumor progression effectively. Through comprehensive analysis and discussion, we strive to pave the way for the development of precision therapies tailored to combat aberrant protein accumulation and improve patient outcomes in cancer.

This Research Topic delves into the intricate interplay between the UPS and cancer progression, with a specific emphasis on TPD as a therapeutic avenue. Contributors are invited to explore various themes, including the mechanisms underlying UPS dysregulation across different cancer types, the roles of E3 ubiquitin ligases in cancer pathogenesis, and the impact of UPS-mediated protein degradation on crucial cellular processes such as cell cycle control, apoptosis, DNA damage response, and cellular signaling. Furthermore, recent advancements in TPD strategies, notably the identification and development of small molecule like molecular glue or PROTACs, hold immense potential for targeted cancer therapy. By integrating insights from molecular biology, genetics, epigenetics, and cellular signaling, this research topic aims to unravel the complexities of UPS-mediated protein degradation in cancer and pave the way for innovative therapeutic interventions. Original research articles, reviews, perspectives, and methodological papers are encouraged, particularly those that contribute novel insights into UPS dysregulation and its therapeutic implications in cancer.

Article types and fees

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

• Brief Research Report
• Data Report
• Editorial
• General Commentary
• Hypothesis and Theory
• Methods
• Mini Review
• Opinion
• Original Research
• ... View all formats

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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
• Data Report
• Editorial
• General Commentary
• Hypothesis and Theory
• Methods
• Mini Review
• Opinion
• Original Research
• Perspective
• Review
• Technology and Code

Keywords: Ubiquitin–Proteasome System, E3 ligases, cell cycle, apoptosis, DNA damage response, cellular signaling

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