AGO2: A Potential Drug Target and Biomarker for Eukaryotic Translation Initiation

Target Name: AGO2

NCBI ID: G27161

AGO2

AGO2: A Potential Drug Target and Biomarker for Eukaryotic Translation Initiation

The process of translation initiation in eukaryotic cells is a critical step in the production of functional proteins. The eukaryotic translation initiation factor 2C (AGO2) is a key protein that plays a crucial role in this process. AGO2 is a 21-kDa protein that is expressed in most eukaryotic cells and is involved in the initiation of protein translation. The identification of potential drug targets and biomarkers for AGO2 is an important area of research with potential implications for the development of new therapeutic approaches.

AGO2 Structure and Function

The AGO2 protein is a member of the HIC (hierarchical interaction domains) family, which are characterized by the presence of multiple domains of varying sizes that are involved in protein-protein interactions. The AGO2 protein has a unique structure that consists of a N-terminal domain of 115 amino acids, a C-terminal domain of 28 amino acids, and a variable region that contains additional amino acids.

The N-terminal domain of AGO2 contains a nucleotide-binding oligomerization domain (NBO), which is responsible for binding to the eukaryotic RNA polymerase II (eRNPII) complex. The NBO domain is composed of the amino acids Asp-21, Asp-22, Asp-23, and Asp-24, which form a nucleotide-binding domain that interacts with the active site of the eRNPII complex. This interaction between AGO2 and eRNPII is critical for the initiation of protein translation.

The C-terminal domain of AGO2 contains a protein-protein interaction domain (PPID) that is involved in the interaction between AGO2 and other proteins. The PPID is composed of the amino acids Asp-25, Asp-26, and Asp-27, which form a protein-protein interaction domain that can interact with the N-terminal domain of AGO2.

The variable region of AGO2 contains additional amino acids that are involved in the interaction between AGO2 and the eRNPII complex. The variable region contains the amino acids Asp-28, Asp-29, Asp-30, Asp-31, Asp-32, and Asp-33, which form a nucleotide-binding domain that interacts with the active site of the eRNPII complex.

AGO2 Functions

The AGO2 protein is involved in the initiation of protein translation by interacting with the eRNPII complex. AGO2 plays a critical role in the regulation of protein translation by the eRNPII complex. The eRNPII complex is a complex that includes the RNA polymerase II (eRNPII), the eRNPII-interactive protein 1 (eRNPII-1), and the eRNPII-interactive protein 2 (eRNPII-2). These proteins form a complex that interacts with the N-terminal domain of AGO2 and can initiate the process of protein translation.

The AGO2 protein is involved in the regulation of the activity of the eRNPII complex by the NBO domain of AGO2. The NBO domain of AGO2 is responsible for binding to the active site of the eRNPII complex and is involved in the regulation of the binding of eRNPII to AGO2. The binding of eRNPII to AGO2 is critical for the initiation of protein translation by the eRNPII complex.

The AGO2 protein is involved in the regulation of the stability of the eRNPII complex by the PPID domain of AGO2. The PPID domain of AGO2 is involved in the interaction between AGO2 and other proteins, including the eRNPII-1 protein. The PPID domain of AGO2 is involved in the regulation of the stability of the eRNPII-1 protein by the eRNPII complex.

Mutations in AGO2

Mutations in the AGO2 gene have been shown to have

Protein Name: Argonaute RISC Catalytic Component 2

Functions: Required for RNA-mediated gene silencing (RNAi) by the RNA-induced silencing complex (RISC). The 'minimal RISC' appears to include AGO2 bound to a short guide RNA such as a microRNA (miRNA) or short interfering RNA (siRNA). These guide RNAs direct RISC to complementary mRNAs that are targets for RISC-mediated gene silencing. The precise mechanism of gene silencing depends on the degree of complementarity between the miRNA or siRNA and its target. Binding of RISC to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by AGO2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation, and this is independent of endonuclease activity. May inhibit translation initiation by binding to the 7-methylguanosine cap, thereby preventing the recruitment of the translation initiation factor eIF4-E. May also inhibit translation initiation via interaction with EIF6, which itself binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit. The inhibition of translational initiation leads to the accumulation of the affected mRNA in cytoplasmic processing bodies (P-bodies), where mRNA degradation may subsequently occur. In some cases RISC-mediated translational repression is also observed for miRNAs that perfectly match the 3' untranslated region (3'-UTR). Can also up-regulate the translation of specific mRNAs under certain growth conditions. Binds to the AU element of the 3'-UTR of the TNF (TNF-alpha) mRNA and up-regulates translation under conditions of serum starvation. Also required for transcriptional gene silencing (TGS), in which short RNAs known as antigene RNAs or agRNAs direct the transcriptional repression of complementary promoter regions

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