Evidence map›Paper›PMID 10388810›Full record

ArticleGenetics1999

Identification and characterization of Schizosaccharomyces pombe asp1(+), a gene that interacts with mutations in the Arp2/3 complex and actin.

A Feoktistova, D McCollum, R Ohi, K L Gould

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
0.2field-weighted citation impact, top 47% 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

22 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
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  4. The Asp1 pyrophosphatase from S. pombe hosts a [2Fe-2S]Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021
    Article
  5. Vip1 is a kinase and pyrophosphatase switch that regulates inositol diphosphate signaling.Proceedings of the National Academy of Sciences of the United States of America · 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

4 authors at 2 institutions in 1 country.

A FeoktistovaHoward Hughes Medical Institute, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, USA.
D McCollum
R Ohi
K L Gould
Howard Hughes Medical Institute · USVanderbilt University · US

Funding

MITOTIC CONTROL GENE CDC28F32GM016145 · NIGMS · VANDERBILT UNIVERSITY · PI MCCOLLUM, DANNEL · 1993 to 1995
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NIGMS NIH HHS GM-16145
6 · The paper itself

Abstract

The Arp2/3 complex is an essential component of the actin cytoskeleton in yeast and is required for the movement of actin patches. In an attempt to identify proteins that interact with this complex in the fission yeast Schizosaccharomyces pombe, we sought high-copy suppressors of the S. pombe arp3-c1 mutant, and have identified one, which we have termed asp1(+). The asp1(+) open reading frame (ORF) predicts a highly conserved protein of 921 amino acids with a molecular mass of 106 kD that does not contain motifs of known function. Neither asp1(+) nor its apparent Saccharomyces cerevisiae ortholog, VIP1, are essential genes. However, disruption of asp1(+) leads to altered morphology and growth properties at elevated temperatures and defects in polarized growth. The asp1 disruption strain also is hypersensitive to Ca+ ions and to low pH conditions. Although Asp1p is not stably associated with the Arp2/3 complex nor localized in any discrete structure within the cytoplasm, the asp1 disruption mutant was synthetically lethal with mutations in components of the Arp2/3 complex, arp3-c1 and sop2-1, as well as with a mutation in actin, act1-48. Moreover, the vip1 disruption strain showed a negative genetic interaction with a las17Delta strain. We conclude that Asp1p/Vip1p is important for the function of the cortical actin cytoskeleton.

Indexed as

Cytoskeletal ProteinsSchizosaccharomyces pombe ProteinsActin-Related Protein 2Actin-Related Protein 3ActinsAmino Acid SequenceCalciumCytoskeletonEndocytosisFungal ProteinsGenes, FungalHydrogen-Ion ConcentrationMolecular Sequence DataMultifunctional EnzymesPhenotypePyrophosphatasesActin-Related Protein 2Actin-Related Protein 3ActinsAsp1 protein, S pombeCalciumCytoskeletal ProteinsFungal ProteinsMultifunctional EnzymesPyrophosphatasesSchizosaccharomyces pombe Proteins

Identifiers

PMID10388810
PMCPMC1460656
OpenAlexW2156768828

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.