Evidence map›Paper›PMID 25254656›Full record

ArticlePLoS genetics2014

The Vip1 inositol polyphosphate kinase family regulates polarized growth and modulates the microtubule cytoskeleton in fungi.

Jennifer Pöhlmann, Carmen Risse, Constanze Seidel, Thomas Pohlmann, Visnja Jakopec, Eva Walla, Pascal Ramrath, Norio Takeshita, Sebastian Baumann, Michael Feldbrügge and 2 more

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed, 64 citations in OpenAlex.

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  12. Mitotic spindle formation in the absence of Polo kinase.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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  15. HJournal of fungi (Basel, Switzerland) · 2021
    Article
  16. 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
  17. Review
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  19. 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
  20. Review
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

12 authors at 2 institutions in 2 countries.

Jennifer PöhlmannLehrstuhl für funktionelle Genomforschung der Mikroorganismen, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.
Carmen RisseLehrstuhl für funktionelle Genomforschung der Mikroorganismen, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.
Constanze SeidelKarlsruhe Institute of Technology (KIT) - South Campus, Institute for Applied Biosciences, Dept. of Microbiology, Karlsruhe, Germany.
Thomas PohlmannInstitut für Mikrobiologie, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.
Visnja JakopecLehrstuhl für funktionelle Genomforschung der Mikroorganismen, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.
Eva WallaLehrstuhl für funktionelle Genomforschung der Mikroorganismen, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.
Pascal RamrathLehrstuhl für funktionelle Genomforschung der Mikroorganismen, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.
Norio TakeshitaKarlsruhe Institute of Technology (KIT) - South Campus, Institute for Applied Biosciences, Dept. of Microbiology, Karlsruhe, Germany; University of Tsukuba, Faculty of Life and Environmental Sciences, Ibaraki, Tsukuba, Japan.
Sebastian BaumannInstitut für Mikrobiologie, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.
Michael FeldbrüggeInstitut für Mikrobiologie, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.
Reinhard FischerKarlsruhe Institute of Technology (KIT) - South Campus, Institute for Applied Biosciences, Dept. of Microbiology, Karlsruhe, Germany.
Ursula FleigLehrstuhl für funktionelle Genomforschung der Mikroorganismen, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.
Heinrich Heine University Düsseldorf · DEKarlsruhe Institute of Technology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microtubules (MTs) are pivotal for numerous eukaryotic processes ranging from cellular morphogenesis, chromosome segregation to intracellular transport. Execution of these tasks requires intricate regulation of MT dynamics. Here, we identify a new regulator of the Schizosaccharomyces pombe MT cytoskeleton: Asp1, a member of the highly conserved Vip1 inositol polyphosphate kinase family. Inositol pyrophosphates generated by Asp1 modulate MT dynamic parameters independent of the central +TIP EB1 and in a dose-dependent and cellular-context-dependent manner. Importantly, our analysis of the in vitro kinase activities of various S. pombe Asp1 variants demonstrated that the C-terminal phosphatase-like domain of the dual domain Vip1 protein negatively affects the inositol pyrophosphate output of the N-terminal kinase domain. These data suggest that the former domain has phosphatase activity. Remarkably, Vip1 regulation of the MT cytoskeleton is a conserved feature, as Vip1-like proteins of the filamentous ascomycete Aspergillus nidulans and the distantly related pathogenic basidiomycete Ustilago maydis also affect the MT cytoskeleton in these organisms. Consistent with the role of interphase MTs in growth zone selection/maintenance, all 3 fungal systems show aspects of aberrant cell morphogenesis. Thus, for the first time we have identified a conserved biological process for inositol pyrophosphates.

Indexed as

Cell ProliferationFungal ProteinsFungiInositol PhosphatesInterphaseMicrotubule-Associated ProteinsMicrotubulesPhosphotransferases (Phosphate Group Acceptor)SchizosaccharomycesFungal Proteinsinositol hexakisphosphate kinaseInositol PhosphatesMicrotubule-Associated ProteinsPhosphotransferases (Phosphate Group Acceptor)

Identifiers

PMID25254656
PMCPMC4177672
OpenAlexW2074836345

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.