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Article

Residues required for phosphorylation of translation initiation factor eIF2α under diverse stress conditions are divergent between yeast and human.

The international journal of biochemistry & cell biology - 1 Feb 2015

Majumder Mithu, Mitchell Daniel, Merkulov Sergei, Wu Jing, Guan Bo-Jhih, Snider Martin D, Krokowski Dawid, Yee Vivien C, Hatzoglou Maria

Abstract excerpt

PERK, PKR, HRI and GCN2 are the four mammalian kinases that phosphorylate the α subunit of the eukaryotic translation initiation factor 2 (eIF2α) on Ser51. This phosphorylation event is conserved among many species and attenuates protein synthesis in response to diverse stress conditions. In contrast, Saccharmyces cerevisiae expresses only the GCN2 kinase. It was demonstrated previously in S. cerevisiae that...

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Identifiers

PMID: 25541374
DOI: 10.1016/j.biocel.2014.12.004
PMCID: PMC4365977

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Residues required for phosphorylation of translation initiation factor eIF2α under diverse stress conditions are divergent between yeast and human.PMID 25541374Read ↗

PKR and GCN2 kinases and guanine nucleotide exchange factor eukaryotic translation initiation factor 2B (eIF2B) recognize overlapping surfaces on eIF2alpha.Semantic proximity Read ↗

The interferon-induced double-stranded RNA-activated protein kinase PKR will phosphorylate serine, threonine, or tyrosine at residue 51 in eukaryotic initiation factor 2alpha.Semantic proximity Read ↗

The highly acidic C-terminal region of the yeast initiation factor subunit 2 alpha (eIF-2 alpha) contains casein kinase phosphorylation sites and is essential for maintaining normal regulation of GCN4.Semantic proximity Read ↗

Regulated translation initiation controls stress-induced gene expression in mammalian cells.Semantic proximity Read ↗

Histidyl-tRNA synthetase-related sequences in GCN2 protein kinase regulate in vitro phosphorylation of eIF-2.Semantic proximity Read ↗

Phosphorylation of translation initiation factor eIF2α at Ser51 depends on site- and context-specific information.Semantic proximity Read ↗

Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2.Semantic proximity Read ↗

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

Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase.Semantic proximity Read ↗

Requirement for kinase-induced conformational change in eukaryotic initiation factor 2alpha (eIF2alpha) restricts phosphorylation of Ser51.Semantic proximity Read ↗

Asp56 in actin is critical for the full activity of the amino acid starvation-responsive kinase Gcn2.Semantic proximity Read ↗

A human kinase yeast array for the identification of kinases modulating phosphorylation-dependent protein-protein interactionsSemantic proximity Read ↗

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