Evidence map›Paper›PMID 11290701›Full record

ArticleGenetics2001

Overexpression of translation elongation factor 1A affects the organization and function of the actin cytoskeleton in yeast.

R Munshi, K A Kandl, A Carr-Schmid, J L Whitacre, A E Adams, T G Kinzy

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

46 citing papers in PubMed, 88 citations in OpenAlex.

  1. Review
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  7. Responses of the MushroomJournal of fungi (Basel, Switzerland) · 2022
    Article
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  9. Review
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  11. International journal of molecular sciences · 2020
    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

6 authors at 3 institutions in 1 country.

R MunshiDepartment of Molecular Genetics and Microbiology, UMDNJ Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA.
K A Kandl
A Carr-Schmid
J L Whitacre
A E Adams
T G Kinzy
University of Arizona · USJohnson University · USRutgers Cancer Institute of New Jersey

Funding

Integrative Cancer Scholars Training GrantT32CA009213 · NCI · UNIVERSITY OF ARIZONA · PI CAREW, JENNIFER S, CURIEL-LEWANDROWSKI, CLARA · 1985 to 2024
$8.6M
Regulators of Translation Elongation Factor eEF1AR01GM057483 · NIGMS · WESTERN MICHIGAN UNIVERSITY · PI KINZY, TERRI GOSS · 1998 to 2017
$5.4M
MOLECULAR ANALYSIS OF THE YEAST ACTIN CYTOSKELETONR01GM045288 · NIGMS · UNIVERSITY OF ARIZONA · PI ADAMS, ALISON E · 1991 to 1999
–
NCI NIH HHS CA09213NIGMS NIH HHS GM45288NIGMS NIH HHS GM57483NIGMS NIH HHS R01 GM057483
6 · The paper itself

Abstract

The translation elongation factor 1 complex (eEF1) plays a central role in protein synthesis, delivering aminoacyl-tRNAs to the elongating ribosome. The eEF1A subunit, a classic G-protein, also performs roles aside from protein synthesis. The overexpression of either eEF1A or eEF1B alpha, the catalytic subunit of the guanine nucleotide exchange factor, in Saccharomyces cerevisiae results in effects on cell growth. Here we demonstrate that overexpression of either factor does not affect the levels of the other subunit or the rate or accuracy of protein synthesis. Instead, the major effects in vivo appear to be at the level of cell morphology and budding. eEF1A overexpression results in dosage-dependent reduced budding and altered actin distribution and cellular morphology. In addition, the effects of excess eEF1A in actin mutant strains show synthetic growth defects, establishing a genetic connection between the two proteins. As the ability of eEF1A to bind and bundle actin is conserved in yeast, these results link the established ability of eEF1A to bind and bundle actin in vitro with nontranslational roles for the protein in vivo.

Indexed as

Saccharomyces cerevisiae ProteinsActinsCell CycleCell DivisionCytoskeletonFungal ProteinsGene ExpressionGenes, FungalPeptide Elongation Factor 1Saccharomyces cerevisiaeActinsFungal ProteinsPeptide Elongation Factor 1Saccharomyces cerevisiae ProteinsTEF1 protein, S cerevisiae

Identifiers

PMID11290701
PMCPMC1461591
OpenAlexW2255636874

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.