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.
An, J, Shi, Y, Hayes, SE, Yang, NN, Sandusky, GE, Stramm, LE, Liang, J
Herbert, TP
Suragani, RN, Ehtesham, NZ, Kamindla, R, Ramaiah, KV
Li, Q, Wang, Z, Tang, Y, Chen, XZ, Yang, J, Liang, G
Wek, RC, Vattem, KM, Ma, K
Koromilas, A, Wouters, BG, Diehl, A, Rastani, S, Koumenis, C, Naczki, C, Sonenberg, N, Koritzinsky, M
protein serine/threonine kinase activity of PERK dimer [endoplasmic reticulum membrane]
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