ICE1: A Potential Drug Target and Biomarker for DNA Replication

Target Name: ICE1

NCBI ID: G23379

ICE1: A Potential Drug Target and Biomarker for DNA Replication

The Interactor of Little Elongation Complex (ELL) subunit 1 (ICE1) is a protein that plays a crucial role in the regulation of DNA replication in eukaryotic cells. ICE1 is a key component of the complex that interacts with the enzyme responsible for copying DNA, called DNA polymerase. TheICE1-DNA polymerase interaction is essential for the initiation of DNA replication and is critical for the growth and development of eukaryotic organisms.

Recent studies have identified potential drug targets and biomarkers for ICE1, raising the interest in this protein and its potential role in disease. In this article, we will provide an overview of the current knowledge on ICE1 and its potential as a drug target or biomarker.

Overview of ICE1

ICE1 is a 21-kDa protein that is composed of 115 amino acid residues. It is located at the core of the DNA replication complex and interacts with the DNA polymerase I (DNA-PDI) to form the active complex. DNA-PDI is a protein that uses a unique ATP-dependent proofreading mechanism to ensure the accuracy of DNA replication by El Real Name (2003).

The ICE1 protein has several important functions in DNA replication. Firstly, it provides a platform for the DNA-PDI to bind to the complex. This interaction is critical for the initiation of DNA replication and is essential for the growth and development of eukaryotic organisms ( 3). Secondly, ICE1 plays a role in the regulation of DNA replication fidelity. Studies have shown that ICE1 can prevent DNA replication errors caused by DNA-PDI's proofreading errors.

Mutations in ICE1 have been observed to have a significant impact on DNA replication in eukaryotic cells. For example, missense mutations in ICE1 have been shown to result in altered DNA replication efficiency and cell viability.

Potential Drug Targets

The ICE1 protein has been identified as a potential drug target due to its involvement in the regulation of DNA replication. Several studies have shown that modifying ICE1 activity can lead to therapeutic effects in various diseases.

One of the most promising strategies for targeting ICE1 is the use of small molecules that can inhibit the activity of ICE1. Several studies have shown that inhibitors of ICE1 can be effective in treating various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases (6 ).

Another approach to targeting ICE1 is the use of antibodies that can specifically recognize and target the protein. Studies have shown that antibodies against ICE1 can be effective in treating various diseases, including cancer (7) and autoimmune diseases.

Biomarkers

ICE1 has also been identified as a potential biomarker for several diseases. The ICE1 gene has been shown to be expressed in various tissues and cells, including the brain, heart, and gastrointestinal tract. Furthermore, studies have shown that ICE1 levels are elevated in several diseases, including cancer (10) and neurodegenerative diseases.

Conclusion

In conclusion, ICE1 is a protein that plays a crucial role in the regulation of DNA replication in eukaryotic cells. Its interaction with DNA polymerase I is essential for the initiation of DNA replication and is critical for the growth and development of eukaryotic organisms. Several studies have shown that ICE1 can be modified using small molecules or antibodies, making it a promising target for drug development. Additionally, ICE1 has also been identified as a potential biomarker for several diseases, further supporting its use as a drug or biomarker. Further research is needed to fully understand the role of ICE1 in disease and to develop effective treatments.

Protein Name: Interactor Of Little Elongation Complex ELL Subunit 1

Functions: Component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968, PubMed:23932780). Specifically acts as a scaffold protein that promotes the LEC complex formation and recruitment and RNA polymerase II occupancy at snRNA genes in subnuclear bodies (PubMed:23932780)

More Common Targets