Regulation of Protein Synthesis in ER: EIF3H's Role and Impact on Disease

Target Name: EIF3H

NCBI ID: G8667

EIF3H

Regulation of Protein Synthesis in ER: EIF3H's Role and Impact on Disease

EIF3H (endoplasmic reticulum-resident factor 3H), also known as eIF3H, is a protein that plays a critical role in the regulation of protein synthesis in the endoplasmic reticulum (ER). The ER is a specialized organelle that plays a crucial role in the folding and processing of proteins, and is responsible for the quality control of the proteins that are exported from the cell. EIF3H is a key regulator of this process, and its dysfunction has been implicated in a number of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

The EIF3H protein is composed of several domains, including an N-terminal transmembrane domain, a coiled-coil domain, and a C-terminal TIR domain. The N-terminal transmembrane domain is responsible for the formation of the protein's cytoplasmic tail, which is important for its ability to interact with other proteins and for its role in cellular signaling. The coiled-coil domain is responsible for the protein's stability and for its ability to interact with other proteins, including other EIF3Hs. The C-terminal TIR domain is responsible for the protein's ability to interact with DNA and for its role in transcriptional regulation.

EIF3H is a key regulator of protein synthesis in the ER. It functions as a negative regulator of the translation of pre-mRNA to protein, by binding to the AUG codon at the start of the mRNA and preventing its initiation of translation. This function is critical for ensuring that only correctly translated and stable proteins are produced and for preventing the production of harmful mutants. In addition to its role in translation regulation, EIF3H is also involved in the regulation of protein degradation, by binding to the protein's own N-terminus and preventing its degradation by the ER-associated degradation pathway.

EIF3H's dysfunction has been implicated in a number of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. For example, studies have shown that EIF3H is often overexpressed or downregulated in cancer cells, and that its dysfunction is associated with the development of cancer-promoting processes. In addition, EIF3H's role in the regulation of protein synthesis has been implicated in a number of neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease. These conditions are characterized by the progressive loss of normal cellular proteins, including those that are regulated by EIF3H, and by the development of neurofibrillary tangles and other pathological hallmarks.

Despite the significant impact of EIF3H's dysfunction on a variety of diseases, its precise mechanism of action is not well understood. However, several studies have identified key interactions between EIF3H and its downstream targets, including the transcription factor NF-kappa-B and the protein involved in the regulation of the cytoskeleton, called Myosin. These studies have provided insight into the molecular mechanisms that underlie EIF3H's function, and have identified potential targets for new therapeutic interventions.

In conclusion, EIF3H is a protein that plays a critical role in the regulation of protein synthesis in the endoplasmic reticulum. Its dysfunction has been implicated in a number of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. Despite the significant impact of EIF3H's dysfunction, its precise mechanism of action is not well understood. Further research is needed to identify potential targets for new therapeutic interventions and to fully understand the role of EIF3H in the regulation of protein synthesis in the ER.

Protein Name: Eukaryotic Translation Initiation Factor 3 Subunit H

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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