Evidence map›Paper›PMID 32303658›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Vip1 is a kinase and pyrophosphatase switch that regulates inositol diphosphate signaling.

D Eric Dollins, Wenli Bai, Peter C Fridy, James C Otto, Julie L Neubauer, Samuel G Gattis, Kavi P M Mehta, John D York

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

55 citing papers in PubMed, 71 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. The Diphosphoinositol Polyphosphate Phosphohydrolase 1 family binds IPInternational journal of biological macromolecules · 2026
    Article
  5. Article
  6. Science advances · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Visualizing and Identifying Inositol Pyrophosphate Isomers in Crystallo.Methods in molecular biology (Clifton, N.J.) · 2025
    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

8 authors at 2 institutions in 1 country.

D Eric DollinsDepartment of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710.
Wenli BaiDepartment of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710.
Peter C FridyDepartment of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710.
James C OttoDepartment of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710.
Julie L NeubauerDepartment of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710.ORCID 0000-0001-8855-1891
Samuel G GattisDepartment of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710.
Kavi P M MehtaDepartment of Biochemistry, Vanderbilt University, Nashville, TN 37232-0146.ORCID 0000-0002-2582-073X
John D YorkDepartment of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710; john.york@vanderbilt.edu.
Duke Medical Center · USVanderbilt University · US

Funding

The Role of Inositol Signaling in Human DiseaseR01HL055672 · NHLBI · WASHINGTON UNIVERSITY · PI YORK, JOHN D. · 1996 to 2012
$5.4M
Inositol hexakisphosphate regulation of N-terminal acetyltransferasesR01GM124404 · NIGMS · VANDERBILT UNIVERSITY · PI YORK, JOHN D. · 2017 to 2020
$1.6M
Howard Hughes Medical InstituteNHLBI NIH HHS R01 HL055672NIGMS NIH HHS R01 GM124404
6 · The paper itself

Abstract

Inositol diphosphates (PP-IPs), also known as inositol pyrophosphates, are high-energy cellular signaling codes involved in nutrient and regulatory responses. We report that the evolutionarily conserved gene product, Vip1, possesses autonomous kinase and pyrophosphatase domains capable of synthesis and destruction of D-1 PP-IPs. Our studies provide atomic-resolution structures of the PP-IP products and unequivocally define that the Vip1 gene product is a highly selective 1-kinase and 1-pyrophosphatase enzyme whose activities arise through distinct active sites. Kinetic analyses of kinase and pyrophosphatase parameters are consistent with Vip1 evolving to modulate levels of 1-IP

Indexed as

DiphosphatesInositol PhosphatesKineticsPhosphorylationPhosphotransferases (Phosphate Group Acceptor)PyrophosphatasesSaccharomyces cerevisiaeSignal TransductionDiphosphatesinositol 2-monophosphateinositol hexakisphosphate kinaseInositol PhosphatesPhosphotransferases (Phosphate Group Acceptor)Pyrophosphatasescell polarityinositol phosphateinositol pyrophosphatekinasephosphatase

Identifiers

PMID32303658
PMCPMC7196807
OpenAlexW3016853697

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.