Evidence map›Paper›PMID 27697865›Full record

ArticleMolecular and cellular biology2016

Inositol Pyrophosphate Kinase Asp1 Modulates Chromosome Segregation Fidelity and Spindle Function in Schizosaccharomyces pombe.

Boris Topolski, Visnja Jakopec, Natascha A Künzel, Ursula Fleig

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-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

14 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. 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
  8. Article
  9. The Key Role of IPMolecules (Basel, Switzerland) · 2020
    Review
  10. 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
  11. Article
  12. Review
  13. Review
  14. 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

4 authors at 1 institution in 1 country.

Boris TopolskiInstitut für Funktionelle Genomforschung der Mikroorganismen, Eukaryotische Mikrobiologie, Heinrich-Heine-Universität, Düsseldorf, Germany.
Visnja JakopecInstitut für Funktionelle Genomforschung der Mikroorganismen, Eukaryotische Mikrobiologie, Heinrich-Heine-Universität, Düsseldorf, Germany.
Natascha A KünzelInstitut für Funktionelle Genomforschung der Mikroorganismen, Eukaryotische Mikrobiologie, Heinrich-Heine-Universität, Düsseldorf, Germany.
Ursula FleigInstitut für Funktionelle Genomforschung der Mikroorganismen, Eukaryotische Mikrobiologie, Heinrich-Heine-Universität, Düsseldorf, Germany fleigu@hhu.de.
Heinrich Heine University Düsseldorf · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chromosome transmission fidelity during mitosis is of critical importance for the fitness of an organism, as mistakes will lead to aneuploidy, which has a causative role in numerous severe diseases. Proper segregation of chromosomes depends on interdependent processes at the microtubule-kinetochore interface and the spindle assembly checkpoint. Here we report the discovery of a new element essential for chromosome transmission fidelity that implicates inositol pyrophosphates (IPPs) as playing a key role in this process. The protein is Asp1, the Schizosaccharomyces pombe member of the highly conserved Vip1 family. Vip1 enzymes are bifunctional: they consist of an IPP-generating kinase domain and a pyrophosphatase domain that uses such IPPs as substrates. We show that Asp1 kinase function is required for bipolar spindle formation. The absence of Asp1-generated IPPs resulted in errors in sister chromatid biorientation, a prolonged checkpoint-controlled delay of anaphase onset, and chromosome missegregation. Remarkably, expression of Asp1 variants that generated higher-than-wild-type levels of IPPs led to a faster-than-wild-type entry into anaphase A without an increase in chromosome missegregation. In fact, the chromosome transmission fidelity of a nonessential chromosome was enhanced with increased cellular IPPs. Thus, we identified an element that optimized the wild-type chromosome transmission process.

Indexed as

Chromosome SegregationChromosomes, FungalCytoskeletal ProteinsInositol PhosphatesKinetochoresMicrotubulesMitosisMultifunctional EnzymesProtein DomainsPyrophosphatasesSchizosaccharomycesSchizosaccharomyces pombe ProteinsSpindle ApparatusAsp1 protein, S pombeCytoskeletal ProteinsInositol PhosphatesMultifunctional EnzymesPyrophosphatasesSchizosaccharomyces pombe Proteins

Identifiers

PMID27697865
PMCPMC5126298
OpenAlexW2528910932

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.