PERK

Supporting information

PKR-like ER kinase (PERK, EIF2AK3), EC 2.7.11.1, is a eukaryotic initiation factor 2α (elF2α) kinase that inhibits protein translation and is important in the endoplasmic reticulum (ER) stress response. PERK is localized to the ER and contains a stress-sensing domain that faces the ER lumen, a transmembrane segment, and a cytosolic kinase domain.

PERK plays an integral role in the unfolded protein response (UPR) and integrated stress response (ISR). The UPR and ISR are activated by a build-up of unfolded proteins in the ER and increase in cellular stressors such as hypoxia, respectively. Induction of these pathways activates PERK by inducing the dissociation of ER chaperones from the stress-sensing domain, resulting in PERK oligomerization and autophosphorylation. Upon activation PERK phosphorylates and inactivates eIF2α, which leads to a global reduction in protein synthesis. As well as suppressing global protein translation, the PERK-dependent inhibition of eIF2α also results in the upregulation of stress-response genes such as ATF4 and the pro-apoptotic protein CHOP (GADD153). This allows the build-up of unfolded proteins to be efficiently processed and promote cell survival during periods of cell stress.

PERK is a useful target for studying diseases associated with UPR and ISR dysfunction. ER stress, hypoxia and aberrant proteins synthesis are all important factors in many major disease states such as cancer, neurodegeneration and diabetes. PERK inhibition has been shown to induce apoptosis and autophagy pathways, therefore PERK inhibitors are potentially useful therapeutic tools for the inhibition of tumorigenesis.

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Gene Species Gene Symbol Gene Accession No. Protein Accession No.
EIF2AK3 Human EIF2AK3 NM_004836 Q9NZJ5
Mouse Eif2ak3 NM_010121 Q9Z2B5
Rat Eif2ak3 NM_031599 NP_113787

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Neuroscience 2016

Neuroscience 2016

November 12 - 16, 2016

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