Evidence map›Paper›PMID 8334302›Full record

ArticleMolecular biology of the cell1993

Unexpected combinations of null mutations in genes encoding the actin cytoskeleton are lethal in yeast.

A E Adams, J A Cooper, D G Drubin

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

34 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Genetically inspired in vitro reconstitution ofMolecular biology of the cell · 2020
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  20. Movement of cortical actin patches in yeast.The Journal of cell biology · 1996
    Article
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 1 institution in 1 country.

A E AdamsDepartment of Molecular and Cellular Biology, Life Sciences South, University of Arizona, Tuscon 85721.
J A Cooper
D G Drubin
University of Arizona · US

Funding

Molecular Analysis of the Yeast Actin CytoskeletonR37GM042759 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI DRUBIN, DAVID G · 2006 to 2015
$4.0M
MOLECULAR ANALYSIS OF THE YEAST ACTIN CYTOSKELETONR01GM042759 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI DRUBIN, DAVID G. · 1989 to 2005
$1.6M
MOLECULAR ANALYSIS OF THE YEAST ACTIN CYTOSKELETONR01GM045288 · NIGMS · UNIVERSITY OF ARIZONA · PI ADAMS, ALISON E · 1991 to 1999
–
NIGMS NIH HHS GM38542NIGMS NIH HHS GM42759NIGMS NIH HHS GM45288
6 · The paper itself

Abstract

To understand the role of the actin cytoskeleton in cell physiology, and how actin-binding proteins regulate the actin cytoskeleton in vivo, we and others previously identified actin-binding proteins in Saccharomyces cerevisiae and studied the effect of null mutations in the genes for these proteins. A null mutation of the actin gene (ACT1) is lethal, but null mutations in the tropomyosin (TPM1), fimbrin (SAC6), Abp1p (ABP1), and capping protein (CAP1 and CAP2) genes have relatively mild or no effects. We have now constructed double and triple mutants lacking 2 or 3 of these actin-binding proteins, and studied the effect of the combined mutations on cell growth, morphology, and organization of the actin cytoskeleton. Double mutants lacking fimbrin and either Abp1p or capping protein show negative synthetic effects on growth, in the most extreme case resulting in lethality. All other combinations of double mutations and the triple mutant lacking tropomyosin, Abp1p, and capping protein, are viable and their phenotypes are similar to or only slightly more severe than those of the single mutants. Therefore, the synthetic phenotypes are highly specific. We confirmed this specificity by overexpression of capping protein and Abp1p in strains lacking fimbrin. Thus, while overexpression of these proteins has deleterious effects on actin organization in wild-type strains, no synthetic phenotype was observed in the absence of fimbrin. We draw two important conclusions from these results. First, since mutations in pairs of actin-binding protein genes cause inviability, the actin cytoskeleton of yeast does not contain a high degree of redundancy. Second, the lack of structural and functional homology among these genetically redundant proteins (fimbrin and capping protein or Abp1p) indicates that they regulate the actin cytoskeleton by different mechanisms. Determination of the molecular basis for this surprising conclusion will provide unique insights into the essential mechanisms that regulate the actin cytoskeleton.

Indexed as

Genes, FungalActin Depolymerizing FactorsActinsCytoskeletonDestrinGenes, LethalMembrane GlycoproteinsMicrofilament ProteinsMicroscopy, FluorescenceMutationPhenotypeSaccharomyces cerevisiaeSuppression, GeneticActin Depolymerizing FactorsActinsDestrinMembrane GlycoproteinsMicrofilament Proteinsplastin

Identifiers

PMID8334302
PMCPMC300950
OpenAlexW2026395694

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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.