Overview of EIF3E: Key Regulator of ER Protein Folding and Localization

Target Name: EIF3E

NCBI ID: G3646

Overview of EIF3E: Key Regulator of ER Protein Folding and Localization

The endoplasmic reticulum (ER) is a complex organellum that plays a crucial role in the proper functioning of eukaryotic cells. It is a dynamic structure that regulates the delivery and processing of cellular components, including proteins. One of the key proteins involved in this process is the endoplasmic reticulum protein EIF3E (endoplasmic reticulum-associated protein EIF3E), which is a key regulator of protein folding and localization in the ER.

In recent years, researchers have made significant progress in the study of EIF3E, and our understanding of its functions and potential as a drug target or biomarker continues to grow. In this article, we will provide an overview of EIF3E, including its structure, function, and potential as a drug target.

Structure

EIF3E is a protein that contains 114 amino acid residues and has a calculated molecular weight of 13.9 kDa. It is a member of the family of transmembrane protein (TMP)s, which are involved in the regulation of protein traffic and localization in various organelles, including the ER. EIF3E is predominantly monomeric and has a linear molecular structure, with four transmembrane domains and one cytoplasmic tail.

The N-terminus of EIF3E is located at the cytoplasmic side of the ER and is responsible for its ability to interact with various cellular components, including the cytoskeleton and various intracellular signaling pathways. The transmembrane domains of EIF3E are located in the ER and are responsible for its ability to interact with the cytoskeleton and various intracellular signaling pathways.

Function

EIF3E is involved in the regulation of protein traffic and localization in the ER. It plays a key role in the delivery of proteins to the ER lumen, where they can be processed and sorted for transport to other cellular organelles. EIF3E is also involved in the regulation of protein interactions with various intracellular signaling pathways, including the PI3K/Akt signaling pathway.

In addition to its role in protein traffic and localization, EIF3E is also involved in the regulation of cellular processes such as cell growth, apoptosis, and stress resistance. It has been shown to play a role in the regulation of cell cycle progression, and is involved in the G1/S transition that occurs during the cell cycle.

As a drug target, EIF3E has the potential to be a target for small molecules that can modulate its activity and improve protein folding and localization in the ER. Additionally, because EIF3E is involved in the regulation of cellular processes such as cell growth, apoptosis, and stress resistance, it may also be a potential biomarker for various diseases, such as cancer and neurodegenerative diseases.

Potential Therapeutic Applications

The potential therapeutic applications for EIF3E are vast and varied. One of the most promising areas of research is the development of small molecules that can modulate EIF3E activity and improve protein folding and localization in the ER. This area of research is in its infancy, and there is a need for further investigation to identify potential lead compounds.

Another potential application of EIF3E is the development of drugs that can inhibit its activity and improve protein traffic and localization in the ER. This could be useful for the treatment of various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases.

In addition to its potential therapeutic applications, EIF3E also has the potential to be a valuable biomarker for various diseases. Its involvement in the regulation of cellular processes such as cell cycle progression, apoptosis, and stress resistance makes it an attractive candidate for the development of biomarkers for these diseases.

Conclusion

EIF3E is a protein that plays a crucial role in the regulation of protein

Protein Name: Eukaryotic Translation Initiation Factor 3 Subunit E

Functions: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773). Required for nonsense-mediated mRNA decay (NMD); may act in conjunction with UPF2 to divert mRNAs from translation to the NMD pathway (PubMed:17468741). May interact with MCM7 and EPAS1 and regulate the proteasome-mediated degradation of these proteins (PubMed:17310990, PubMed:17324924)

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