PERK
Protein kinase RNA-like endoplasmic reticulum kinase (PERK; EC 2.7.11.1) is a type I ER membrane protein and one of three (next to IRE1 and ATF6) primary effectors of the unfolded protein response (UPR), which has a demonstrated role in tumor growth and angiogenesis. Increase in unfolded proteins in the ER causes release of ER chaperones from the stress-sensing domain of PERK, which results in its activation via oligomerization and autophosphorylation at multiple serine, threonine, and tyrosine residues. Upon activation, PERK phosphorylates eukaryotic initiation factor 2α (eIF2α), rendering it an inhibitor of the ribosome translation initiation complex, consequently reducing overall protein synthesis. The reduction in translation reduces the ER burden, providing time for the cell to process or degrade the accumulated unfolded proteins to restore ER homeostasis[1].
[1] J.M. Axten et al. Discovery of 7-methyl-5-(1-{[3-(trifluoromethyl)phenyl]acetyl}-2,3-dihydro-1H-indol-5-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine (GSK2606414), a potent and selective first-in-class inhibitor of protein kinase R (PKR)-like endoplasmic reticulum kinase (PERK). J. Med. Chem. 2012, 55, 7193-7207.
| Axon ID | Name | Description | From price | |
|---|---|---|---|---|
| 2233 | GSK 2606414 | Potent and selective inhibitor of PERK (EIF2AK3) | €99.00 | |
| 2278 | ISRIB | Potent inhibitor of the integrated stress response and PERK signaling | €95.00 | |