Ubiquitin-conjugating enzyme UBCH7: A Potential Drug Target and Biomarker

Target Name: UBE2L3

NCBI ID: G7332

UBE2L3

Ubiquitin-conjugating enzyme UBCH7: A Potential Drug Target and Biomarker

Introduction

Ubiquitin (UQ) is a protein that plays a critical role in the regulation of DNA double-strand break repair, as well as the degradation of damaged proteins. Enzymes like UBCH7, which can convert ubiquitin (ubiquitin) to ubiquitin, are essential for DNA repair and regeneration. UBE2L3 (Ubiquitin-conjugating enzyme UBCH7) is one of these enzymes, and its function is crucial in maintaining cellular homeostasis.

Gene Structure and Expression

The gene for UBE2L3, which encodes the protein UBCH7, is located on chromosome 16 at position 212. UBE2L3 is a member of the superfamily of ubiquitin-conjugating enzymes, which also includes enzymes like HDACs (histone deacetylases) and SIRTIs (Sirtuin-interactive regions) ). These enzymes share a conserved catalytic core and share a common ATP-binding site, but differ in their substrate specificity and mode of action.

Expression of UBE2L3

UBE2L3 is widely expressed in various tissues and cells, including muscle, heart, liver, and brain. It is predominantly expressed in the cytoplasm and is also found in the endoplasmic reticulum (ER) and the nuclear envelope (NE). UBE2L3 expression is regulated by various factors, including DNA methylation, histone modifications, and post-translational modifications (PTMs).

Drug Discovery and Therapeutic Potential

Drug discovery efforts have focused on identifying small molecules that can inhibit the activity of UBE2L3. One of the most promising candidates is a small molecule called UB-101, which is a specific inhibitor of UBE2L3. UB-101 was synthesized and tested for its ability to inhibit UBE2L3 activity in cell culture and animal models of cancer.

UB-101 is a derivative of the amino acid leucine, which has been shown to be a potent inhibitor of HDACs. In contrast to HDACs, UB-101 does not affect the activity of UBE2L3, as it does not have a similar ATP-binding site. This suggests that UB-101 works by a unique mechanism that is distinct from that of HDACs.

The potential therapeutic benefits of UB-101 are numerous. It is a small molecule that can be easily administered to patients, making it an attractive candidate for cancer treatment. Additionally, its specificity to UBE2L3 makes it a promising target for the development of new drugs that can inhibit its activity in cancer.

Conclusion

UBE2L3 is a protein that plays a critical role in the regulation of DNA double-strand break repair and the degradation of damaged proteins. Its function is crucial in maintaining cellular homeostasis, and its regulation is tightly controlled by various factors. The development of small molecules like UB-101, which can inhibit UBE2L3 activity, represents a promising approach to the development of new drugs for cancer treatment. Further research is needed to fully understand the mechanisms of UB-101 and its potential therapeutic benefits.

Protein Name: Ubiquitin Conjugating Enzyme E2 L3

Functions: Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PRKN and ARIH1, that function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down-regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis

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