Evidence map›Paper›PMID 17178834›Full record

ArticleMolecular and cellular biology2007

Improper organization of the actin cytoskeleton affects protein synthesis at initiation.

Stephane R Gross, Terri Goss Kinzy

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

54 citing papers in PubMed, 94 citations in OpenAlex.

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  16. Article
  17. Review
  18. Article
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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 1 institution in 1 country.

Stephane R GrossDepartment of Molecular Genetics, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway, NJ 08854, USA.
Terri Goss Kinzy
Rutgers, The State University of New Jersey · US

Funding

Regulators of Translation Elongation Factor eEF1AR01GM057483 · NIGMS · WESTERN MICHIGAN UNIVERSITY · PI KINZY, TERRI GOSS · 1998 to 2017
$5.4M
Structure of Eukaryotic Translation Elongation Factor 1R01GM062789 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI KINZY, TERRI GOSS · 2001 to 2004
$883k
NIGMS NIH HHS GM57483NIGMS NIH HHS GM62789NIGMS NIH HHS R01 GM057483NIGMS NIH HHS R01 GM062789
6 · The paper itself

Abstract

Although the actin cytoskeleton and the translation machinery are considered to be separate cellular complexes, growing evidence supports overlapping regulation of the two systems. Because of its interaction with actin, the eukaryotic translation elongation factor 1A (eEF1A) is proposed to be a regulator or link between these processes. Using a genetic approach with the yeast Saccharomyces cerevisiae, specific regions of eEF1A responsible for actin interactions and bundling were identified. Five new mutations were identified along one face of eEF1A. Dramatic changes in cell growth, cell morphology, and actin cable and patch formation as well as a unique effect on total translation in strains expressing the F308L or S405P eEF1A mutant form were observed. The translation effects do not correlate with reduced translation elongation but instead include an initiation defect. Biochemical analysis of the eEF1A mutant forms demonstrated reduced actin-bundling activity in vitro. Reduced total translation and/or the accumulation of 80S ribosomes in strains with either a mutation or a null allele of genes encoding actin itself or actin-regulating proteins Tpm1p, Mdm20p, and Bnirp/Bni1p was observed. Our data demonstrate that eEF1A, other actin binding proteins, and actin mutants affect translation initiation through the actin cytoskeleton.

Indexed as

Protein BiosynthesisActinsAllelesCytoskeletonModels, MolecularMutationPeptide Elongation Factor 1Protein Structure, TertiaryRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsActinsPeptide Elongation Factor 1Recombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID17178834
PMCPMC1820457
OpenAlexW2029789860

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.