EID1(EP300 interacting inhibitor of differentiation 1) is a member of the EID protein family, which regulates differentiation, transcription and acetyltransferase activity. EID1 function was originally identified as a transcriptional repressor which regulates cell cycle and differentiation, and leads to genome inactivation and instability by interacting with E3 ubiquitin ligase MDM2. EID1 is mainly located in the cytoplasm. It was translocated into the nuclei under stressed or pathological conditions such as AD patients and APP Tg mice brains.
The eukaryotic translation initiation factor 2-α subunit (EIF2S1) is the first regulatory step that catalyzes the initiation of protein synthesis and promotes the binding of the initial tRNA to the 40S ribosomal subunit. As an important translation initiation factor, the eukaryotic initiation factor 2-α subunit is regulated by a variety of signal molecules, that is, it functions by regulating the phosphorylation and acetylation status of EIF2S1. Kinases activated by viral infection (PKR), endoplasmic reticulum stress (PERK/PEK), amino acid deprivation (GCN2) or heme deficiency (HRI) can phosphorylate EIF2S1 to regulate the transcription and translation of cell-related genes and enhance Cell protection mechanism.
The translation initiation factor EIF2 catalyzes the first regulated step of protein synthesis initiation, promoting the binding of the initiator tRNA to 40S ribosomal subunits. Binding occurs as a ternary complex of methionyl-tRNA, EIF2, and GTP. EIF2 is composed of 3 nonidentical subunits, the 36-kD EIF2-alpha subunit (EIF2S1), the 38-kD EIF2-beta subunit (EIF2S2; MIM 603908), and the 52-kD EIF2-gamma subunit (EIF2S3; MIM 300161). The rate of formation of the ternary complex is modulated by the phosphorylation state of EIF2-alpha (Ernst et al., 1987 [PubMed 2948954]).
RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. 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. 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. UniRule annotation4 Publications (Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2.
eIF3 is a large translation initiation complex with 10 to 13 different subunits. eIF3A, eIF3B, eIF3C, eIF3E, eIF3F, and eIF3H are the core subunits critical for the function of this complex. eIF3 physically interacts with eIF4G, which may be responsible for the association of the 40S ribosomal subunit with mRNA. eIF3 also stabilizes the binding of Met-tRNAf.eIF2.GTP to the 40S ribosomal subunit and helps keep the integrity of the resulting complex upon addition of the 60S ribosomal subunit. Studies have shown that mTOR interacts with eIF3 directly. When cells are stimulated by hormones or mitogenic signals, mTOR binds to the eIF3 complex and phosphorylates S6K1. This process results in the dissociation of S6K1 from eIF3 and S6K1 activation. The activated S6K1 then phosphorylates its downstream targets including ribosomal protein S6 and eIF4B, resulting in stimulation of translation. Further findings demonstrated that activated mTOR signaling induces the association of eIF3 with eIF4G upon stimulation with insulin.
Eukaryotic initiation factor 4A (eIF4A) has an essential role in the binding of mRNA to the 43S preinitiation complex when protein synthesisbegins, as eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the smallribosomal subunit, and subsequent scanning for the initiator codon.
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