Evidence map›Paper›PMID 30201631›Full record

ReviewJournal of lipid research2019

Signaling through non-membrane nuclear phosphoinositide binding proteins in human health and disease.

Jamal M Bryant, Raymond D Blind

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of lipid research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

19 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Review
  3. Structural Rationalization of IPMK Inhibitor Potency.Journal of medicinal chemistry · 2025
    Article
  4. The Inner Nuclear Membrane Has a Unique Lipid Signature.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. SF-1 Induces Nuclear PIP2.Biomolecules · 2023
    Article
  14. Article
  15. Review
  16. Review
  17. The nuclear phosphoinositide response to stress.Cell cycle (Georgetown, Tex.) · 2020
    Review
  18. Review
  19. Nuclear Phosphoinositides: Their Regulation and Roles in Nuclear Functions.International journal of molecular sciences · 2019
    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

2 authors at 1 institution in 1 country.

Jamal M BryantDepartments of Pharmacology, Biochemistry, and Medicine, Division of Diabetes, Endocrinology, and Metabolism, Vanderbilt Diabetes Research and Training Center, Vanderbilt University School of Medicine, Nashville, TN 37232.
Raymond D BlindDepartments of Pharmacology, Biochemistry, and Medicine, Division of Diabetes, Endocrinology, and Metabolism, Vanderbilt Diabetes Research and Training Center, Vanderbilt University School of Medicine, Nashville, TN 37232 ray.blind@vanderbilt.edu.ORCID 0000-0002-1358-6309
Vanderbilt University · US

Funding

User Training and OutreachP30GM124169 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI Gregory L Hura · 2017 to 2026
$28.6M
MULTIDISCIPLINARY TRAINING IN MOLECULAR ENDOCRINOLOGYT32DK007563 · NIDDK · VANDERBILT UNIVERSITY · PI Richard M O'Brien · 1988 to 2026
$15.9M
Vanderbilt/Meharry Initiative for Minority Student DvptR25GM062459 · NIGMS · VANDERBILT UNIVERSITY · PI VELEZ EDWARDS, DIGNA R · 2002 to 2020
$10.4M
NIDDK NIH HHS T32 DK007563NIGMS NIH HHS P30 GM124169NIGMS NIH HHS R25 GM062459
6 · The paper itself

Abstract

Phosphoinositide membrane signaling is critical for normal physiology, playing well-known roles in diverse human pathologies. The basic mechanisms governing phosphoinositide signaling within the nucleus, however, have remained deeply enigmatic owing to their presence outside the nuclear membranes. Over 40% of nuclear phosphoinositides can exist in this non-membrane state, held soluble in the nucleoplasm by nuclear proteins that remain largely unidentified. Recently, two nuclear proteins responsible for solubilizing phosphoinositides were identified, steroidogenic factor-1 (SF-1; NR5A1) and liver receptor homolog-1 (LRH-1; NR5A2), along with two enzymes that directly remodel these phosphoinositide/protein complexes, phosphatase and tensin homolog (PTEN; MMAC) and inositol polyphosphate multikinase (IPMK; ipk2). These new footholds now permit the assignment of physiological functions for nuclear phosphoinositides in human diseases, such as endometriosis, nonalcoholic fatty liver disease/steatohepatitis, glioblastoma, and hepatocellular carcinoma. The unique nature of nuclear phosphoinositide signaling affords extraordinary clinical opportunities for new biomarkers, diagnostics, and therapeutics. Thus, phosphoinositide biology within the nucleus may represent the next generation of low-hanging fruit for new drugs, not unlike what has occurred for membrane phosphatidylinositol 3-kinase drug development. This review connects recent basic science discoveries in nuclear phosphoinositide signaling to clinical pathologies, with the hope of inspiring development of new therapies.

Indexed as

DiseaseHealthSignal TransductionAnimalsHumansPhosphatidylinositolsReceptors, Cytoplasmic and NuclearPhosphatidylinositolsReceptors, Cytoplasmic and Nucleardiabetesendometriosisglioblastomahepatocellular carcinomainositol phosphate multikinasenuclear lipid signalingphosphatidylinositol (3,4,5) triphosphate

Identifiers

PMID30201631
PMCPMC6358298
OpenAlexW2891317111

What Socratic 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 Socratic graph.