Evidence map›Paper›PMID 24550313›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

SAC phosphoinositide phosphatases at the tonoplast mediate vacuolar function in Arabidopsis.

Petra Nováková, Sibylle Hirsch, Elena Feraru, Ricardo Tejos, Ringo van Wijk, Tom Viaene, Mareike Heilmann, Jennifer Lerche, Riet De Rycke, Mugurel I Feraru and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
14.9field-weighted citation impact, top 1% 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

33 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
  3. TheeLife · 2022
    Article
  4. Article
  5. Article
  6. Review
  7. Tonoplast-localized CaProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
  9. LPIAT, aInternational journal of molecular sciences · 2020
    Article
  10. Article
  11. DownregulatingFrontiers in plant science · 2020
    Article
  12. The Function of Inositol Phosphatases in Plant Tolerance to Abiotic Stress.International journal of molecular sciences · 2019
    Review
  13. Polar vacuolar distribution is essential for accurate asymmetric division ofProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. Review
  15. Review
  16. Phosphoinositides control the localization of HOPS subunit VPS41, which together with VPS33 mediates vacuole fusion in plants.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  17. ArabidopsisPlant physiology · 2018
    Article
  18. Article
  19. Article
  20. 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

15 authors at 5 institutions in 4 countries.

Petra NovákováInstitute of Science and Technology Austria, 3400 Klosterneuburg, Austria.
Sibylle Hirsch
Elena Feraru
Ricardo Tejos
Ringo van Wijk
Tom Viaene
Mareike Heilmann
Jennifer Lerche
Riet De Rycke
Mugurel I Feraru
Peter Grones
Marc Van Montagu
Ingo Heilmann
Teun Munnik
Jirí Friml
Ghent University · BEMartin Luther University Halle-Wittenberg · DEVlaams Instituut voor Biotechnologie · BENetherlands Institute for Neuroscience · NLInstitute of Science and Technology Austria · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphatidylinositol (PtdIns) is a structural phospholipid that can be phosphorylated into various lipid signaling molecules, designated polyphosphoinositides (PPIs). The reversible phosphorylation of PPIs on the 3, 4, or 5 position of inositol is performed by a set of organelle-specific kinases and phosphatases, and the characteristic head groups make these molecules ideal for regulating biological processes in time and space. In yeast and mammals, PtdIns3P and PtdIns(3,5)P2 play crucial roles in trafficking toward the lytic compartments, whereas the role in plants is not yet fully understood. Here we identified the role of a land plant-specific subgroup of PPI phosphatases, the suppressor of actin 2 (SAC2) to SAC5, during vacuolar trafficking and morphogenesis in Arabidopsis thaliana. SAC2-SAC5 localize to the tonoplast along with PtdIns3P, the presumable product of their activity. In SAC gain- and loss-of-function mutants, the levels of PtdIns monophosphates and bisphosphates were changed, with opposite effects on the morphology of storage and lytic vacuoles, and the trafficking toward the vacuoles was defective. Moreover, multiple sac knockout mutants had an increased number of smaller storage and lytic vacuoles, whereas extralarge vacuoles were observed in the overexpression lines, correlating with various growth and developmental defects. The fragmented vacuolar phenotype of sac mutants could be mimicked by treating wild-type seedlings with PtdIns(3,5)P2, corroborating that this PPI is important for vacuole morphology. Taken together, these results provide evidence that PPIs, together with their metabolic enzymes SAC2-SAC5, are crucial for vacuolar trafficking and for vacuolar morphology and function in plants.

Indexed as

ArabidopsisArabidopsis ProteinsDNA PrimersEvolution, MolecularMicroscopy, Electron, TransmissionPhenotypePhosphatidylinositol PhosphatesPhosphoprotein PhosphatasesPlants, Genetically ModifiedReal-Time Polymerase Chain ReactionVacuolesArabidopsis ProteinsDNA PrimersPhosphatidylinositol PhosphatesPhosphoprotein Phosphatasesepidermal cellsmembrane fusion and fissionmembrane lipids

Identifiers

PMID24550313
PMCPMC3932866
OpenAlexW1991869583

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.