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Article

Ser-64 and Ser-111 in PHAS-I are dispensable for insulin-stimulated dissociation from eIF4E.

The Journal of biological chemistry - 28 Nov 2003

Ferguson Gail, Mothe-Satney Isabelle, Lawrence John C

Abstract excerpt

Insulin stimulates phosphorylation of multiple sites in the eIF4E-binding protein, PHAS-I, leading to dissociation of the PHAS-I.eIF4E complex and to an increase in cap-dependent translation. The Ser-64 and Ser-111 sites have been proposed to have key roles in controlling the association of PHAS-I and eIF4E. To determine whether the effects of insulin require these sites, we assessed the control of PHAS-I...

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Identifiers

PMID: 14507920
DOI: 10.1074/jbc.M307949200

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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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Ser-64 and Ser-111 in PHAS-I are dispensable for insulin-stimulated dissociation from eIF4E.PMID 14507920Read ↗

Multiple mechanisms control phosphorylation of PHAS-I in five (S/T)P sites that govern translational repression.Semantic proximity Read ↗

The C terminus of initiation factor 4E-binding protein 1 contains multiple regulatory features that influence its function and phosphorylation.Semantic proximity Read ↗

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

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

A role for PYK2 in ANG II-dependent regulation of the PHAS-1-eIF4E complex by multiple signaling cascades in vascular smooth muscle.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 eukaryotic initiation factor 4E (eIF4E) at Ser209 is not required for protein synthesis in vitro and in vivo.Semantic proximity Read ↗

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

Two phosphorylation sites on eIF-2 alpha.Semantic proximity Read ↗

Insulin induces phosphorylation of serine residues of translationally controlled tumor protein in 293T cells.Semantic proximity Read ↗

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