EIF3F-HUMAN: A Potential Drug Target and Biomarker (G8665)

Target Name: EIF3F

NCBI ID: G8665

EIF3F

EIF3F-HUMAN: A Potential Drug Target and Biomarker

Eukaryotic introns are a type of RNA molecule that play a critical role in gene expression and are highly conserved across various organisms. EIF3F, a protein found in various cellular compartments, has been identified as a potential drug target and biomarker. Its function and structure have been extensively studied, and its potential as a drug target continue to attract researchers' interest.

EIF3F: Structure and Function

The protein encoded by the EIF3F gene is a 21-kDa protein that contains 115 amino acid residues. It is composed of a unique N-terminal transmembrane region, a cytoplasmic tail, and a unique C-terminal region involved in protein-protein interactions. EIF3F functions as a protein scaffold, which allows it to interact with various protein partners, including transcription factors, thereby regulating gene expression.

The N-terminal transmembrane region of EIF3F contains a unique farnesylated cysteine residue, which is crucial for its stability and functions as a protein scaffold. This cysteine residue is also involved in the regulation of EIF3F's stability and interacts with various protein partners, including the nuclear protein p21.

The cytoplasmic tail of EIF3F is composed of a unique GFP-like region and a series of basic amino acids, which plays a role in its stability and localization to various cellular compartments.

The C-terminal region of EIF3F is involved in protein-protein interactions and contains a unique GXXG repeat, which is known for its role in protein stability and interaction. This C-terminal region also contains a unique lysine residue that is involved in protein-protein interactions and may contribute to EIF3F's stability.

EIF3F's Potential as a Drug Target

EIF3F has been identified as a potential drug target due to its unique structure and function. Its N-terminal transmembrane region and cysteine residue make it a potential target for small molecules or antibodies that can modulate its stability or activity. Additionally, its cytoplasmic tail and GFP-like region make it a potential target for imaging techniques, such as GFP-based live cell imaging.

EIF3F has also been shown to play a critical role in the regulation of cell cycle progression and has been linked to various cellular processes, including cell division, apoptosis, and inflammation. Therefore, targeting EIF3F may be a promising strategy for treating various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases.

EIF3F as a Biomarker

EIF3F has also been identified as a potential biomarker for various diseases. Its unique structure and function make it an attractive target for diagnostic tools, such as mass spectrometry-based proteomic analysis. For example, researchers have used EIF3F as a biomarker to diagnose various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases.

Conclusion

EIF3F is a unique protein that has been extensively studied for its structure and function. Its N-terminal transmembrane region, cysteine residue, and C-terminal region have been shown to play critical roles in its stability and interaction with various protein partners. Its potential as a drug target and biomarker continues to attract researchers' interest. Further research is needed to fully understand the mechanisms of EIF3F's function and its potential as a drug and biomarker.

Protein Name: Eukaryotic Translation Initiation Factor 3 Subunit F

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)

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•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
•   disease relevance;
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•   related combination drugs;
•   pharmacochemistry experiments;
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•   advantages and risks of development, etc.
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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