Evidence map›Paper›PMID 39531477›Full record

ArticlePLoS genetics2024

Inositol pyrophosphate catabolism by three families of phosphatases regulates plant growth and development.

Florian Laurent, Simon M Bartsch, Anuj Shukla, Felix Rico-Resendiz, Daniel Couto, Christelle Fuchs, Joël Nicolet, Sylvain Loubéry, Henning J Jessen, Dorothea Fiedler and 1 more

Abstract read
In one paragraph

Article in PLoS genetics, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Science advances · 2026
    Article
  6. Affinity-Based Interactome Mapping of Inositol Pyrophosphates Reveals 4/6-PP-InsPAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  7. Article
  8. Article
  9. EstablishingAnalytical chemistry · 2025
    Article
  10. Article
  11. mBio · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. 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

11 authors.

Florian LaurentStructural Plant Biology Laboratory, Department of Plant Sciences, University of Geneva, Geneva, Switzerland.
Simon M BartschDepartment of Chemical Biology, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany.ORCID https://orcid.org/0000-0002-2215-7901
Anuj ShuklaInstitute of Organic Chemistry, University of Freiburg, Freiburg, Germany.ORCID https://orcid.org/0000-0002-4154-689X
Felix Rico-ResendizStructural Plant Biology Laboratory, Department of Plant Sciences, University of Geneva, Geneva, Switzerland.
Daniel CoutoStructural Plant Biology Laboratory, Department of Plant Sciences, University of Geneva, Geneva, Switzerland.
Christelle FuchsPlant Imaging Unit, Department of Plant Sciences, University of Geneva, Geneva, Switzerland.ORCID https://orcid.org/0000-0001-8181-2294
Joël NicoletStructural Plant Biology Laboratory, Department of Plant Sciences, University of Geneva, Geneva, Switzerland.
Sylvain LoubéryPlant Imaging Unit, Department of Plant Sciences, University of Geneva, Geneva, Switzerland.ORCID https://orcid.org/0000-0001-7061-9456
Henning J JessenInstitute of Organic Chemistry, University of Freiburg, Freiburg, Germany.
Dorothea FiedlerDepartment of Chemical Biology, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany.
Michael HothornStructural Plant Biology Laboratory, Department of Plant Sciences, University of Geneva, Geneva, Switzerland.ORCID https://orcid.org/0000-0002-3597-5698

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inositol pyrophosphates (PP-InsPs) are nutrient messengers whose cellular levels are precisely regulated. Diphosphoinositol pentakisphosphate kinases (PPIP5Ks) generate the active signaling molecule 1,5-InsP8. PPIP5Ks harbor phosphatase domains that hydrolyze PP-InsPs. Plant and Fungi Atypical Dual Specificity Phosphatases (PFA-DSPs) and NUDIX phosphatases (NUDTs) are also involved in PP-InsP degradation. Here, we analyze the relative contributions of the three different phosphatase families to plant PP-InsP catabolism. We report the biochemical characterization of inositol pyrophosphate phosphatases from Arabidopsis and Marchantia polymorpha. Overexpression of different PFA-DSP and NUDT enzymes affects PP-InsP levels and leads to stunted growth phenotypes in Arabidopsis. nudt17/18/21 knock-out mutants have altered PP-InsP pools and gene expression patterns, but no apparent growth defects. In contrast, Marchantia polymorpha Mppfa-dsp1ge, Mpnudt1ge and Mpvip1ge mutants display severe growth and developmental phenotypes and associated changes in cellular PP-InsP levels. Analysis of Mppfa-dsp1geand Mpvip1ge mutants supports a role for PP-InsPs in Marchantia phosphate signaling, and additional functions in nitrate homeostasis and cell wall biogenesis. Simultaneous elimination of two phosphatase activities enhanced the observed growth phenotypes. Taken together, PPIP5K, PFA-DSP and NUDT inositol pyrophosphate phosphatases regulate growth and development by collectively shaping plant PP-InsP pools.

Indexed as

ArabidopsisInositol PhosphatesPhosphoric Monoester HydrolasesArabidopsis ProteinsGene Expression Regulation, PlantPhosphotransferases (Phosphate Group Acceptor)Plant DevelopmentPyrophosphatasesArabidopsis Proteinsdiphosphoinositol pentakisphosphate kinaseinositol-1-pyrophosphateInositol PhosphatesPhosphoric Monoester HydrolasesPhosphotransferases (Phosphate Group Acceptor)Pyrophosphatases

Identifiers

PMID39531477
PMCPMC11611267

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Registered trials

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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.