EIF2AK3 (PERK) phosphorylates EIF2S1 (eIF2-alpha)Phosphorylation of eIF2-alpha by PERK

Stable Identifier
Reaction [transition]
Homo sapiens
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The C-terminal domain of PERK (EIF2AK3) has kinase activity when PERK homodimerizes. PERK kinase specifically phosphorylates Ser52 of eIF2-alpha, causing an arrest in translation. The result is that translation of ER-targeted proteins is halted on ribosomes in the vicinity of activated PERK. The general arrest of translation results in the loss of short-lived proteins such as Cyclin D1, causing an arrest of the cell cycle in G1.

Literature References
PubMed ID Title Journal Year
10026192 Characterization of a mutant pancreatic eIF-2alpha kinase, PEK, and co-localization with somatostatin in islet delta cells

An, J, Shi, Y, Hayes, SE, Yang, NN, Sandusky, GE, Stramm, LE, Liang, J

J Biol Chem 1999
17956313 PERK in the life and death of the pancreatic beta-cell

Herbert, TP

Biochem Soc Trans 2007
16288713 Interaction of recombinant human eIF2 subunits with eIF2B and eIF2alpha kinases

Suragani, RN, Ehtesham, NZ, Kamindla, R, Ramaiah, KV

Biochem Biophys Res Commun 2005
18664456 Polycystin-2 down-regulates cell proliferation via promoting PERK-dependent phosphorylation of eIF2alpha

Li, Q, Wang, Z, Tang, Y, Chen, XZ, Yang, J, Liang, G

Hum Mol Genet 2008
11907036 Dimerization and release of molecular chaperone inhibition facilitate activation of eukaryotic initiation factor-2 kinase in response to endoplasmic reticulum stress

Wek, RC, Vattem, KM, Ma, K

J Biol Chem 2002
12370288 Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha

Koromilas, A, Wouters, BG, Diehl, A, Rastani, S, Koumenis, C, Naczki, C, Sonenberg, N, Koritzinsky, M

Mol Cell Biol 2002
Catalyst Activity

protein serine/threonine kinase activity of PERK dimer [endoplasmic reticulum membrane]

Orthologous Events
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