Eif2 Alpha is an important component in the neurobiology of neurodegenerative diseases. This page provides detailed information about its structure, function, and role in disease processes.
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|+ **eIF2 Alpha**
! Protein Name
| eIF2 Alpha
! Gene
| [EIF2S1](/genes/eif2s1)
! UniProt ID
| [P05198](https://www.uniprot.org/uniprot/P05198)
! PDB IDs
| 1VSG, 1VS6
! Molecular Weight
| 36.1 kDa
! Subcellular Localization
| Cytoplasm
! Protein Family
| eIF2 alpha subunit family
eIF2 Alpha (EIF2S1) is a protein involved in protein synthesis and ribosome function. It is located in the cytoplasm and participates in critical cellular pathways.
eIF2-alpha has a domain structure that interacts with eIF2B.
eIF2-alpha is the alpha subunit of the eIF2 complex, which delivers the initiator Met-tRNA to the ribosome. Phosphorylation of eIF2-alpha at Ser51 by PERK, GCN2, PKR, and HRI inhibits global translation but promotes expression of specific stress-response genes.
eIF2-alpha phosphorylation is a hallmark of the integrated stress response in AD, PD, and ALS. Chronic phosphorylation contributes to synaptic failure.
ISRIB (Integrated Stress Response Inhibitor) reverses eIF2-alpha phosphorylation effects and is being studied for cognitive enhancement.
The study of Eif2 Alpha has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.
- Ron D et al. (2007) Translational control in stress. Cell 128(2):233-238. PMID: 17254960
- Proud CG (2005) eIF2 and its phosphorylation. Trends Biochem Sci 30(2):105-108. PMID: 15694925
- Baird TD et al. (2009) eIF2alpha phosphorylation in stress. Cold Spring Harb Perspect Biol 1(6):a004945. PMID: 20066104
- Costa-Mattioli M et al. (2009) eIF2alpha phosphorylation in memory. Nature 457(7229):891-895. PMID: 19078956
- Moreno JA et al. (2012) eIF2alpha phosphorylation in neurodegeneration. J Clin Invest 122(11):3935-3942. PMID: 23114593
- Ma T et al. (2013) eIF2alpha in Alzheimer's disease. Nat Rev Neurosci 14(4):233-238. PMID: 23552214
- Hughes MP et al. (2020) eIF2alpha in ALS. Acta Neuropathol Commun 8(1):136. PMID: 32799840
- Way KP et al. (2018) Integrated stress response in neurodegeneration. Neurobiol Dis 109(Pt B):191-200. PMID: 28428079
- Ron D et al. (2007) Translational control in stress. Cell 128(2):233-238. PMID: 17254960
- Proud CG (2005) eIF2 and its phosphorylation. Trends Biochem Sci 30(2):105-108. PMID: 15694925
- Baird TD et al. (2009) eIF2alpha phosphorylation in stress. Cold Spring Harb Perspect Biol 1(6):a004945. PMID: 20066104
- Costa-Mattioli M et al. (2009) eIF2alpha phosphorylation in memory. Nature 457(7229):891-895. PMID: 19078956
- Moreno JA et al. (2012) eIF2alpha phosphorylation in neurodegeneration. J Clin Invest 122(11):3935-3942. PMID: 23114593
- Ma T et al. (2013) eIF2alpha in Alzheimer's disease. Nat Rev Neurosci 14(4):233-238. PMID: 23552214
- Hughes MP et al. (2020) eIF2alpha in ALS. Acta Neuropathol Commun 8(1):136. PMID: 32799840
- Way KP et al. (2018) Integrated stress response in neurodegeneration. Neurobiol Dis 109(Pt B):191-200. PMID: 28428079