Phosphorylation of eIF2-alpha by PERK

Reviewed: D'Eustachio, P, Matthews, L, Gillespie, ME, 2008-12-02 16:25:31 Reviewed: Urano, F, 2010-04-30 The C-terminal domain of PERK 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. Authored: May, B, 2009-06-02 00:51:49 Edited: May, B, 2009-06-02 00:51:49

http://purl.obolibrary.org/obo/HINO_0008889

Reviewed: D'Eustachio, P, Matthews, L, Gillespie, ME, 2008-12-02 16:25:31

Reviewed: Urano, F, 2010-04-30

The C-terminal domain of PERK 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.

Authored: May, B, 2009-06-02 00:51:49

Edited: May, B, 2009-06-02 00:51:49

Pubmed18664456

Pubmed16288713

Reactome, http://www.reactome.org

Pubmed17956313

Pubmed12370288

Pubmed11907036

Pubmed10026192

http://purl.obolibrary.org/obo/CHEBI_15422

http://purl.obolibrary.org/obo/UniProt_P05198

http://purl.obolibrary.org/obo/CHEBI_16761

http://purl.obolibrary.org/obo/UniProt_P05198

Phosphorylation of eIF2-alpha by PERK

HINO:0008889

Phosphorylation of eIF2-alpha by PERK

Reactome Database ID Release 43381111

ReactomeREACT_18275

EC Number: 2.7.11

http://purl.obolibrary.org/obo/INO_0000040