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Article

Modulation of the eukaryotic initiation factor 2 alpha-subunit kinase PERK by tyrosine phosphorylation.

The Journal of biological chemistry - 4 Jan 2008

Su Qiaozhu, Wang Shuo, Gao Hong Qing, Kazemi Shirin, Harding Heather P, Ron David, Koromilas Antonis E

Abstract excerpt

The endoplasmic reticulum (ER)-resident protein kinase PERK attenuates protein synthesis in response to ER stress through the phosphorylation of translation initiation factor eIF2alpha at serine 51. ER stress induces PERK autophosphorylation at several serine/threonine residues, a process that is required for kinase activation and phosphorylation of eIF2alpha. Herein, we demonstrate that PERK also possesses...

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Source

Identifiers

PMID: 17998206
DOI: 10.1074/jbc.M704612200

Genes

ATF4

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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