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Insulin-like growth factor binding protein-5 (IGFBP-5) and protein family member IGFBP-3 upregulate expression of growth arrest and DNA damage-inducible protein 34 (GADD34), which assembles an eIF2[alpha] dephosphorylation complex, enabling regeneration of active eIF2, critical to ternary complex formation
Phosphorylation of the alpha subunit of eIF2 (eIF2[alpha]) blocks ternary complex formation, thereby blocking formation of the 43S preinitiation complex and suppressing global translation.
The mechanisms by which the 43 S complex interacts with translational initiation sites are poorly understood, except for the requirement for the Met-tRNA anticodon and evidence for involvement of eIF2 (6).
Phosphorylation of the [alpha]-subunit of eIF2 is a well-documented mechanism of downregulation of protein synthesis under various stress conditions.
Results: CPT regulated genes related to UPR and eIF2 signaling pathways.
[sup], The eIF2B complex is essential for protein synthesis with the function of guanine nucleotide exchange factor (GEF) activity, converting eIF2 from an inactive GDP-bound structure to an active GTP-bound form.
They found that glucose deprivation caused an increase in BACE1 levels and led to the phosphorylation of the stress-inducible translation initiation factor, eIF2.
Differential activation of eIF2 kinases in response to cellular stresses in Schizosaccharomyces pombe.
For instance, SGs induced by glucose deprivation contain eukaryotic initiation factor eIF4E and eIF4G proteins, mRNAs, and the poly(A)-binding protein Pab1 [12,13], whereas SGs induced by oxidative stress have distinct major components such as eIF2 and downstream factors .
In addition to the modification or cleavage of ribosomal RNA, a variety of ribosome-inactivating stresses lead to phosphorylation of serine 51 on the alpha subunit of eukaryotic translation initiation factor 2 (eIF2), leading to global translational arrest .
One specific mechanism that may be particularly relevant to the blood-forming cells is the control of the initiation factor eIF2 by phosphorylation, which is stimulated by nitric oxide, thus leading to decreased protein synthesis, presumably including the porphyrin biosynthetic enzymes (Urea et al.
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- Eierlegende Woll Milch Sau
- Eierlegende Wollmilchsau
- eIF-1A X isoform
- eIF-1A Y isoform
- eIF-2C 1
- eIF-2C 2
- eIF-2C 3
- eIF-2C 4
- eIF2C 1
- eIF2C 2
- eIF2C 3
- eIF2C 4