eukaryotic initiation factor eIF2 binding

Definition

Target type: molecularfunction

Binding to eukaryotic initiation factor eIF2, a protein complex involved in the initiation of ribosome-mediated translation. [GOC:hjd]

Eukaryotic initiation factor 2 (eIF2) binding is a critical step in the initiation of protein synthesis in eukaryotes. eIF2 is a heterotrimeric protein composed of three subunits: α, β, and γ. The α subunit is the target of phosphorylation, which regulates the activity of eIF2. eIF2 binds to the initiator methionine tRNA (Met-tRNAiMet) and escorts it to the small ribosomal subunit (40S). The eIF2-Met-tRNAiMet complex then interacts with the mRNA and the large ribosomal subunit (60S) to form the 80S initiation complex. eIF2 binding is regulated by several factors, including:

- **Phosphorylation of the α subunit:** Phosphorylation of eIF2α by kinases such as PERK, GCN2, and PKR inhibits eIF2 activity, leading to a decrease in protein synthesis. This is a key mechanism for stress response in cells, as it allows cells to conserve energy and resources when they are under stress.
- **Availability of Met-tRNAiMet:** The availability of Met-tRNAiMet is also critical for eIF2 binding.
- **Interaction with other initiation factors:** eIF2 interacts with other initiation factors, such as eIF1, eIF1A, and eIF5, to facilitate the formation of the initiation complex.

The interaction between eIF2 and its binding partners is highly dynamic and regulated, ensuring the efficient and accurate translation of mRNA into proteins. This process is essential for cell growth, development, and survival.'
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Proteins (1)

Compounds (1)