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Article

Abrogation of translation initiation factor eIF-2 phosphorylation causes malignant transformation of NIH 3T3 cells.

The EMBO journal - 1 Aug 1995

Donzé O, Jagus R, Koromilas A E, Hershey J W, Sonenberg N

Abstract excerpt

The interferon induced double-stranded RNA-activated kinase, PKR, has been suggested to act as a tumor suppressor since expression of a dominant negative mutant of PKR causes malignant transformation. However, the mechanism of transformation has not been elucidated. PKR phosphorylates translation initiation factor eIF-2 alpha on Ser51, resulting in inhibition of protein synthesis and cell growth arrest....

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Identifiers

PMID: 7641700
DOI: 10.1002/j.1460-2075.1995.tb00052.x
PMCID: PMC394457

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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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Abrogation of translation initiation factor eIF-2 phosphorylation causes malignant transformation of NIH 3T3 cells.PMID 7641700Read ↗

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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 ↗

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

Double-stranded-RNA-activated protein kinase PKR enhances transcriptional activation by tumor suppressor p53.Semantic proximity Read ↗

Mechanism of interferon action: evidence for intermolecular autophosphorylation and autoactivation of the interferon-induced, RNA-dependent protein kinase PKR.Semantic proximity Read ↗

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Human interferon-gamma mRNA autoregulates its translation through a pseudoknot that activates the interferon-inducible protein kinase PKR.Semantic proximity Read ↗

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