Evidence map›Paper›PMID 24706853›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Protein phosphatase PP1/GLC7 interaction domain in yeast eIF2γ bypasses targeting subunit requirement for eIF2α dephosphorylation.

Margarito Rojas, Anne-Claude Gingras, Thomas E Dever

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.1field-weighted citation impact, top 23% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Circadian Control of Protein Synthesis.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 2 countries.

Margarito RojasLaboratory of Gene Regulation and Development, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.
Anne-Claude Gingras
Thomas E Dever
Eunice Kennedy Shriver National Institute of Child Health and Human Development · USMount Sinai Hospital · CA

Funding

Mechanism and Regulation of Eukaryotic Protein SynthesisZIAHD001010 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI DEVER, THOMAS E · 2009 to 2025
$29.4M
Intramural NIH HHS
6 · The paper itself

Abstract

Whereas the protein kinases GCN2, HRI, PKR, and PERK specifically phosphorylate eukaryotic translation initiation factor 2 (eIF2α) on Ser51 to regulate global and gene-specific mRNA translation, eIF2α is dephosphorylated by the broadly acting serine/threonine protein phosphatase 1 (PP1). In mammalian cells, the regulatory subunits GADD34 and CReP target PP1 to dephosphorylate eIF2α; however, as there are no homologs of these targeting subunits in yeast, it is unclear how GLC7, the functional homolog of PP1 in yeast, is recruited to dephosphorylate eIF2α. Here, we show that a novel N-terminal extension on yeast eIF2γ contains a PP1-binding motif (KKVAF) that enables eIF2γ to pull down GLC7 and target it to dephosphorylate eIF2α. Truncation or point mutations designed to eliminate the KKVAF motif in eIF2γ impair eIF2α dephosphorylation in vivo and in vitro and enhance expression of GCN4. Replacement of the N terminus of eIF2γ with the GLC7-binding domain from GAC1 or fusion of heterologous dimerization domains to eIF2γ and GLC7, respectively, maintained eIF2α phosphorylation at basal levels. Taken together, these results indicate that, in contrast to the paradigm of distinct PP1-targeting or regulatory subunits, the unique N terminus of yeast eIF2γ functions in cis to target GLC7 to dephosphorylate eIF2α.

Indexed as

AnimalsEukaryotic Initiation Factor-2HumansPhosphorylationProtein BindingProtein Phosphatase 1Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsEukaryotic Initiation Factor-2GIP1 protein, S cerevisiaeProtein Phosphatase 1Saccharomyces cerevisiae Proteins

Identifiers

PMID24706853
PMCPMC3986135
OpenAlexW2066509694

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.