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E3 ligases: a potential multi-drug target for different types of cancers and neurological disorders
Konda Mani Saravanan1, Muthu Kannan2, Prabhakar Meera3
1Research and Development Wing, Bharath Institute of Higher Education and Research, Chennai, 600073, Tamil Nadu, India.
Abstract:
Ubiquitylation is a posttranslational modification of proteins that is necessary for a variety of cellular processes. E1 ubiquitin activating enzyme, E2 ubiquitin conjugating enzyme, and E3 ubiquitin ligase are all involved in transferring ubiquitin to the target substrate to regulate cellular function. The objective of this review is to provide an overview of different aspects of E3 ubiquitin ligases that can lead to major biological system failure in several deadly diseases. The first part of this review covers the important characteristics of E3 ubiquitin ligases and their classification based on structural domains. Further, the authors provide some online resources that help researchers explore the data relevant to the enzyme. The following section delves into the involvement of E3 ubiquitin ligases in various diseases and biological processes, including different types of cancer and neurological disorders.
Insights
E3 ubiquitin ligases are crucial for cellular processes and disease. This review explores their characteristics, classification, and roles in diseases like cancer and neurological disorders, offering resources for researchers.
Area of Science:
- Biochemistry
- Molecular Biology
- Cellular Biology
Background:
- Ubiquitylation is a vital posttranslational protein modification essential for numerous cellular functions.
- The ubiquitin-proteasome system, involving E1, E2, and E3 enzymes, regulates protein degradation and cellular signaling.
- E3 ubiquitin ligases play a critical role in substrate specificity within this pathway.
Purpose of the Study:
- To provide a comprehensive overview of E3 ubiquitin ligases.
- To explore their structural characteristics and classification.
- To detail their involvement in major diseases and biological system failures.
Main Methods:
- Literature review of E3 ubiquitin ligase functions and disease associations.
- Classification of E3 ligases based on structural domains.
- Identification and curation of online data resources for researchers.
Main Results:
- Detailed characterization of E3 ubiquitin ligase families and their structural domains.
- Explanation of the enzymatic cascade for ubiquitin transfer to target proteins.
- Identification of E3 ligase dysregulation in cancers and neurological disorders.
Conclusions:
- E3 ubiquitin ligases are key regulators implicated in the pathogenesis of severe diseases.
- Understanding E3 ligase biology is crucial for developing therapeutic strategies.
- Online resources can facilitate further research into E3 ubiquitin ligase functions and disease relevance.
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