Evidence map›Paper›PMID 24936063›Full record

ArticleThe Journal of biological chemistry2014

Translation elongation factor 1A mutants with altered actin bundling activity show reduced aminoacyl-tRNA binding and alter initiation via eIF2α phosphorylation.

Winder B Perez, Terri Goss Kinzy

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

10 citing papers in PubMed, 21 citations in OpenAlex.

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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

2 authors at 2 institutions in 1 country.

Winder B Perez
Terri Goss Kinzy
Johnson University · USRutgers, The State University of New Jersey · US

Funding

UMDNJ-RUTGERS UNIVERSITY PIPELINE PROGRAMR25GM055145 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI HAIMOVICH, BEATRICE, LANGER, JEROME ALAN · 1996 to 2020
$8.7M
Regulators of Translation Elongation Factor eEF1AR01GM057483 · NIGMS · WESTERN MICHIGAN UNIVERSITY · PI KINZY, TERRI GOSS · 1998 to 2017
$5.4M
VIRUS-HOST INTERACTIONS IN EUKARYOTIC CELLST32AI007403 · NIAID · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI BREWER, GARY A. · 1991 to 2014
$1.7M
NIAID NIH HHS T32 AI007403NIAID NIH HHS T32AI007403NIGMS NIH HHS GM57483NIGMS NIH HHS R01 GM057483NIGMS NIH HHS R25 GM055145
6 · The paper itself

Abstract

Apart from its canonical function in translation elongation, eukaryotic translation elongation factor 1A (eEF1A) has been shown to interact with the actin cytoskeleton. Amino acid substitutions in eEF1A that reduce its ability to bind and bundle actin in vitro cause improper actin organization in vivo and reduce total translation. Initial in vivo analysis indicated the reduced translation was through initiation. The mutant strains exhibit increased levels of phosphorylated initiation factor 2α (eIF2α) dependent on the presence of the general control non-derepressible 2 (Gcn2p) protein kinase. Gcn2p causes downregulation of total protein synthesis at initiation in response to increases in deacylated tRNA levels in the cell. Increased levels of eIF2α phosphorylation are not due to a general reduction in translation elongation as eEF2 and eEF3 mutants do not exhibit this effect. Deletion of GCN2 from the eEF1A actin bundling mutant strains revealed a second defect in translation. The eEF1A actin-bundling proteins exhibit changes in their elongation activity at the level of aminoacyl-tRNA binding in vitro. These findings implicate eEF1A in a feedback mechanism for regulating translation at initiation.

Indexed as

MutationActinsEukaryotic Initiation Factor-2Peptide Chain Elongation, TranslationalPeptide Elongation Factor 1PhosphorylationProtein BindingProtein Serine-Threonine KinasesRNA, FungalRNA, Transfer, Amino AcylSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsActinsEukaryotic Initiation Factor-2GCN2 protein, S cerevisiaePeptide Elongation Factor 1Protein Serine-Threonine KinasesRNA, FungalRNA, Transfer, Amino AcylSaccharomyces cerevisiae Proteins

Identifiers

PMID24936063
PMCPMC4110299
OpenAlexW2070535531

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.