Unlocking the Potential of EIF4A-3: A Drug Target and Biomarker for treatable Paralysis

Target Name: EIF4A3

NCBI ID: G9775

EIF4A3

Unlocking the Potential of EIF4A-3: A Drug Target and Biomarker for treatable Paralysis

Introduction

Paralysis is a debilitating neurological disorder that affects millions of people worldwide, primarily affecting children. It is characterized by muscle weakness and stiffness, making it difficult for individuals to perform daily activities. There are various types of paralysis, including spinal cord injuries, peripheral neuropathy , and myasthenia gravis. Although several treatments have been developed to manage paralysis, the condition remains a significant public health issue.

The discovery of the EIF4A-3 protein, an essential enzyme for the production of ATP-dependent RNA helicase, offers a new potential drug target and biomarker for the treatment of paralysis. EIF4A-3 plays a crucial role in the regulation of protein synthesis, which is essential for muscle growth and maintenance. In this article, we will explore the structure, function, and potential therapeutic applications of EIF4A-3, as well as its potential as a drug target and biomarker for treating paralysis.

Structure and Function

The EIF4A-3 protein is a 21 kDa protein that belongs to the family of ATP-dependent RNA helicases (ADHs). It is expressed in various tissues, including muscle, heart, brain, and kidney. EIF4A-3 is composed of a N -terminal alpha-helices, a catalytic alpha-helices, and a C-terminal T-loop.

The EIF4A-3 protein functions as the ATP-dependent RNA helicase eIF4A-3. This enzyme uses ATP to convert RNA strands into double-stranded RNA (dsRNA). The double-stranded RNA can then be translated into proteins, which are essential for muscle growth and maintenance.

The EIF4A-3 protein is highly conserved, with only a minor difference in the localization of the catalytic active site. This conservation is important for its function as a drug target, as any changes in the EIF4A-3 protein structure can affect its function and potentially lead to the development of drug resistance.

Potential Therapeutic Applications

The discovery of EIF4A-3 as a potential drug target and biomarker for paralysis opens up new avenues for therapeutic development. One of the main goals of drug development is to improve muscle strength and function in individuals with paralysis. By targeting EIF4A-3, researchers could develop small molecules or antibodies that specifically interact with the protein and enhance its function.

For example, researchers could target EIF4A-3 to increase muscle strength and reduce muscle stiffness. This could be achieved by blocking the activity of EIF4A-3 or by inhibiting its interactions with other proteins. Additionally, EIF4A-3 could be used as a biomarker to monitor the effectiveness of therapeutic interventions.

The EIF4A-3 protein is also a promising candidate for targeting EIF4A-3 in the treatment of other neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. These conditions are characterized by the progressive loss of brain cells, leading to a range of symptoms, including cognitive decline, tremors, and muscle stiffness.

Conclusion

In conclusion, the discovery of EIF4A-3 as a potential drug target and biomarker for paralysis offers a promising new direction in the development of therapeutic interventions for this debilitating condition. By targeting the EIF4A-3 protein, researchers could develop small molecules or antibodies that enhance its function and improve muscle strength and function in individuals with paralysis. Further research is needed to fully understand the potential of EIF4A-3 as a drug target and biomarker for paralysis.

Protein Name: Eukaryotic Translation Initiation Factor 4A3

Functions: ATP-dependent RNA helicase (PubMed:16170325). Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:22961380, PubMed:28502770, PubMed:28076346, PubMed:29301961). Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs (PubMed:16209946, PubMed:16170325, PubMed:16314458, PubMed:16923391, PubMed:16931718, PubMed:19033377, PubMed:20479275). The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by CASC3, but abolished in presence of the MAGOH-RBM8A heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGOH-RBM8A heterodimer increases the RNA-binding affinity of the EJC. Involved in translational enhancement of spliced mRNAs after formation of the 80S ribosome complex. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Shows higher affinity for single-stranded RNA in an ATP-bound core EJC complex than after the ATP is hydrolyzed. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly (PubMed:22203037). Involved in craniofacial development (PubMed:24360810)

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•   expression level;
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The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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