Target Name: CBLL2
NCBI ID: G158506
Other Name(s): E3 ubiquitin-protein ligase ZNF645 | E3 ubiquitin-protein ligase CBLL2 | E3 ubiquitin ligase | c-Cbl-like protein 2 | cbl proto-oncogene-like protein 2 | Cbl proto-oncogene like 2 | CT138 | Cbl proto-oncogene-like protein 2 | HAKAIL | RING-type E3 ubiquitin transferase ZNF645 | ZNF645 | CBLL2_HUMAN | zinc finger protein 645 | Zinc finger protein 645 | ZN645_HUMAN

CBLL2: A Potential Drug Target and Biomarker for Ubiquitin-Protein Ligase E3

Introduction

Ubiquitin (ubiquitin-protein ligase) is a vital protein that plays a crucial role in regulating various cellular processes. It is involved in the assembly and disassembly of protein-protein interactions, which are essential for protein function and cell survival. The protein ubiquitin has has been implicated in numerous diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. Therefore, the development of drugs that can specifically target ubiquitin-protein ligase (E3) has become an attractive research direction. In this article, we focus on CBLL2, a potential drug target and biomarker for E3 ubiquitin-protein ligase.

CBLL2: A Putative Drug Target

The ubiquitin-protein ligase E3 is a key enzyme in the ubiquitin system, which is responsible for the covalent attachment of ubiquitin to target proteins. Activated E3 ubiquitin-protein ligase (E3- Ubq) forms a covalent complex with its substrate, leading to the formation of a covalent bond and the formation of a new ubiquitin-protein complex. E3- Ubq is a potent enzyme that can cross-react with a wide variety of proteins, including its own E2 ubiquitin-protein ligase (E2- Ubq) and other E3 ubiquitin-protein ligases. Therefore, targeting E3- Ubq has been challenging.

CBLL2, a gene encoding a protein with potential relevance to E3 ubiquitin-protein ligase, has been identified as a potential drug target. CBLL2 is a 21-kDa protein that is expressed in various tissues, including brain, heart, and muscle. It is Highly conserved and has a low molecular weight, which suggests a nontoxic and biologically active form. CBLL2 has been shown to have a critical role in the regulation of cellular processes, including cell adhesion, migration, and invasion.

CBLL2 has been shown to interact with various proteins, including E2- Ubq, which suggests a potential role for CBLL2 in the ubiquitin system. Additionally, CBLL2 has been shown to interact with the protein ubiquitin-associated DNA damage repair complex (UADC), which is involved in the repair of DNA damage caused by environmental stressors, such as radiation and chemicals.

CBLL2 as a Biomarker

The development of biomarkers for drug targets is an essential step in the drug discovery process. CBLL2, as a potential drug target, could be used as a biomarker for assessing the efficacy of drugs that target E3 ubiquitin-protein ligase (E3- Ubq). For example, if a drug is able to inhibit the activity of CBLL2, it should lead to a decrease in the amount of E3- Ubq that can be formed. This decrease in E3- Ubq formation could be measured by a variety of techniques, including Western blot analysis or immunofluorescence.

In addition to its potential use as a drug biomarker, CBLL2 may also be used as a biomarker for tracking the efficacy of cancer therapies that target E3 ubiquitin-protein ligase (E3- Ubq). For example, if a cancer treatment is able to reduce the amount of E3- Ubq that can be formed, this reduction in E3- Ubq formation could be measured by a variety of techniques, including Western blot analysis or immunofluorescence.

Conclusion

In conclusion, CBLL2 is a potential drug target and biomarker for E3 ubiquitin-protein ligase (E3- Ubq). Its conserved sequence and low molecular weight provide the possibility for its practical application. By inhibiting the activity of CBLL2, the production of E3-Ubq can be reduced, thus providing a promising drug research direction for the development of specific CBLL2 inhibitors.

Protein Name: Cbl Proto-oncogene Like 2

Functions: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (PubMed:20657603). May operate on tyrosine-phosphorylated SRC substrates (PubMed:22252131)

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