Evidence map›Paper›PMID 31248120›Full record

ReviewInternational journal of molecular sciences2019

Nuclear Phosphoinositides: Their Regulation and Roles in Nuclear Functions.

R Fiume, I Faenza, B Sheth, A Poli, M C Vidalle, C Mazzetti, S H Abdul, F Campagnoli, M Fabbrini, S T Kimber and 6 more

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

37 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Review
  3. The Inner Nuclear Membrane Has a Unique Lipid Signature.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  4. Review
  5. Article
  6. Review
  7. ERM proteins support perinuclear actin rim formation.Frontiers in cell and developmental biology · 2025
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. PI3Kα Translocation Mediates Nuclear PtdIns(3,4,5)PMolecular & cellular proteomics : MCP · 2023
    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

16 authors at 3 institutions in 2 countries.

R FiumeDepartment of Biomedical Sciences (DIBINEM), University of Bologna, Via Irnerio, 48, 40126 Bologna, Italy. roberta.fiume@unibo.it.
I FaenzaDepartment of Biomedical Sciences (DIBINEM), University of Bologna, Via Irnerio, 48, 40126 Bologna, Italy. irene.faenza2@unibo.it.ORCID 0000-0002-5227-3567
B ShethInositide Laboratory, School of Biological Sciences, Faculty of Environmental and Life Sciences, University of Southampton, Life Sciences Building 85, Highfield, Southampton SO17 1BJ, UK. B.Sheth@soton.ac.uk.
A PoliIstituto FIRC di Oncologia Molecolare (IFOM), 20139 Milan, Italy. alessandro.poli@ifom.eu.
M C VidalleInositide Laboratory, School of Biological Sciences, Faculty of Environmental and Life Sciences, University of Southampton, Life Sciences Building 85, Highfield, Southampton SO17 1BJ, UK. Magdalena.Castellano-Vidalle@soton.ac.uk.
C MazzettiDepartment of Biomedical Sciences (DIBINEM), University of Bologna, Via Irnerio, 48, 40126 Bologna, Italy. cristina.mazzetti13@gmail.com.
S H AbdulInositide Laboratory, School of Biological Sciences, Faculty of Environmental and Life Sciences, University of Southampton, Life Sciences Building 85, Highfield, Southampton SO17 1BJ, UK. S.Abdul-Hamid@soton.ac.uk.
F CampagnoliInositide Laboratory, School of Biological Sciences, Faculty of Environmental and Life Sciences, University of Southampton, Life Sciences Building 85, Highfield, Southampton SO17 1BJ, UK. f.campagnoli@soton.ac.uk.
M FabbriniDepartment of Biomedical Sciences (DIBINEM), University of Bologna, Via Irnerio, 48, 40126 Bologna, Italy. marco.fabbrini3@studio.unibo.it.ORCID 0000-0003-1431-0643
S T KimberInositide Laboratory, School of Biological Sciences, Faculty of Environmental and Life Sciences, University of Southampton, Life Sciences Building 85, Highfield, Southampton SO17 1BJ, UK. S.T.Kimber@soton.ac.uk.
G A MarianiDepartment of Biomedical Sciences (DIBINEM), University of Bologna, Via Irnerio, 48, 40126 Bologna, Italy. adalgisa.mariani@unibo.it.
J XianDepartment of Biomedical Sciences (DIBINEM), University of Bologna, Via Irnerio, 48, 40126 Bologna, Italy. jie.xian2@unibo.it.
M V MarviDepartment of Biomedical Sciences (DIBINEM), University of Bologna, Via Irnerio, 48, 40126 Bologna, Italy. mariavittoria.marvi@studio.unibo.it.
S MongiorgiDepartment of Biomedical Sciences (DIBINEM), University of Bologna, Via Irnerio, 48, 40126 Bologna, Italy. s.mongiorgi@unibo.it.
Z ShahInositide Laboratory, School of Biological Sciences, Faculty of Environmental and Life Sciences, University of Southampton, Life Sciences Building 85, Highfield, Southampton SO17 1BJ, UK. zash1000@yahoo.com.
N DivechaInositide Laboratory, School of Biological Sciences, Faculty of Environmental and Life Sciences, University of Southampton, Life Sciences Building 85, Highfield, Southampton SO17 1BJ, UK. n.divecha@soton.ac.uk.
University of Bologna · ITUniversity of Southampton · GBIFOM · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polyphosphoinositides (PPIns) are a family of seven lipid messengers that regulate a vast array of signalling pathways to control cell proliferation, migration, survival and differentiation. PPIns are differentially present in various sub-cellular compartments and, through the recruitment and regulation of specific proteins, are key regulators of compartment identity and function. Phosphoinositides and the enzymes that synthesise and degrade them are also present in the nuclear membrane and in nuclear membraneless compartments such as nuclear speckles. Here we discuss how PPIns in the nucleus are modulated in response to external cues and how they function to control downstream signalling. Finally we suggest a role for nuclear PPIns in liquid phase separations that are involved in the formation of membraneless compartments within the nucleus.

Indexed as

Lipid MetabolismAnimalsCell NucleusChemical PhenomenaComputational BiologyHumansIntranuclear SpaceMetabolic Networks and PathwaysNuclear EnvelopePhosphatidylinositol 4,5-DiphosphatePhosphatidylinositolsSignal TransductionPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositolsdemixingepigenetic signallinglipid kinaseliquid-liquid phase separationnucleusphosphoinositidesphospholipase CPtdIns(4,5)P2PtdIns5P

Identifiers

PMID31248120
PMCPMC6627530
OpenAlexW2952666635

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.