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Article

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

Molecular and cellular biology - 1 Apr 2005

Dey Madhusudan, Trieselmann Bruce, Locke Emily G, Lu Jingfang, Cao Chune, Dar Arvin C, Krishnamoorthy Thanuja, Dong Jinsheng, Sicheri Frank, Dever Thomas E

Abstract excerpt

Four stress-responsive protein kinases, including GCN2 and PKR, phosphorylate eukaryotic translation initiation factor 2alpha (eIF2alpha) on Ser51 to regulate general and gene-specific protein synthesis. Phosphorylated eIF2 is an inhibitor of its guanine nucleotide exchange factor, eIF2B. Mutations that block translational regulation were isolated throughout the N-terminal OB-fold domain in Saccharomyces...

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Identifiers

PMID: 15798194
DOI: 10.1128/MCB.25.8.3063-3075.2005
PMCID: PMC1069625

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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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PKR and GCN2 kinases and guanine nucleotide exchange factor eukaryotic translation initiation factor 2B (eIF2B) recognize overlapping surfaces on eIF2alpha.PMID 15798194Read ↗

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

Critical contacts between the eukaryotic initiation factor 2B (eIF2B) catalytic domain and both eIF2beta and -2gamma mediate guanine nucleotide exchange.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 ↗

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

Tight binding of the phosphorylated alpha subunit of initiation factor 2 (eIF2alpha) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation.Semantic proximity Read ↗

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

The beta/Gcd7 subunit of eukaryotic translation initiation factor 2B (eIF2B), a guanine nucleotide exchange factor, is crucial for binding eIF2 in vivo.Semantic proximity Read ↗

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

Sugar phosphate activation of the stress sensor eIF2B.Semantic proximity Read ↗

Baculovirus protein PK2 subverts eIF2α kinase function by mimicry of its kinase domain C-lobe.Semantic proximity Read ↗

Substrate recruitment via eIF2γ enhances catalytic efficiency of a holophosphatase that terminates the Integrated Stress ResponseSemantic proximity Read ↗

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