Source:http://www.reactome.org/biopax/48887BiochemicalReaction1727
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Authored: May, B, 2009-06-02 00:51:49,
Edited: May, B, 2009-06-02 00:51:49,
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.
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| biopax3:xref |
http://identifiers.org/pubmed/10026192,
http://identifiers.org/pubmed/11907036,
http://identifiers.org/pubmed/12370288,
http://identifiers.org/pubmed/16288713,
http://identifiers.org/pubmed/17956313,
http://identifiers.org/pubmed/18664456,
urn:biopax:UnificationXref:REACTOME DATABASE ID_381111,
urn:biopax:UnificationXref:REACTOME_REACT_18275_2
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Phosphorylation of eIF2-alpha by PERK
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2.7.11
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