Evidence map›Paper›PMID 31776069›Full record

ReviewAdvances in biological regulation2020

A two-way switch for inositol pyrophosphate signaling: Evolutionary history and biological significance of a unique, bifunctional kinase/phosphatase.

Thomas A Randall, Chunfang Gu, Xingyao Li, Huanchen Wang, Stephen B Shears

Open access · greenAbstract readReview
In one paragraph

Review in Advances in biological regulation, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

27 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Article
  3. Oncometabolite 5-IPNature chemical biology · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Fluorination Influences the Bioisostery of Myo-Inositol Pyrophosphate Analogs.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Insulin Signal Transduction Perturbations in Insulin Resistance.International journal of molecular sciences · 2021
    Review
  19. New structural insights reveal an expanded reaction cycle for inositol pyrophosphate hydrolysis by human DIPP1.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  20. Inositol phosphate kinases in the eukaryote landscape.Advances in biological regulation · 2021
    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

5 authors at 1 institution in 1 country.

Thomas A RandallIntegrative Bioinformatics Support Group, National Institute of Environmental Health Sciences, NIH, Research Triangle Park, NC 27709, USA.
Chunfang GuSignal Transduction Laboratory, National Institute of Environmental Health Sciences, NIH, Research Triangle Park, NC 27709, USA.
Xingyao LiSignal Transduction Laboratory, National Institute of Environmental Health Sciences, NIH, Research Triangle Park, NC 27709, USA.
Huanchen WangSignal Transduction Laboratory, National Institute of Environmental Health Sciences, NIH, Research Triangle Park, NC 27709, USA.
Stephen B ShearsSignal Transduction Laboratory, National Institute of Environmental Health Sciences, NIH, Research Triangle Park, NC 27709, USA. Electronic address: shears@niehs.nih.gov.
National Institute of Environmental Health Sciences · US

Funding

Inositol SignallingZIAES080046 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI SHEARS, STEPHEN B · 2009 to 2023
$31.3M
REGULATION OF INOSITOL LIPID SIGNALLING MECHANISMSZ01ES080046 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI SHEARS, STEPHEN B · 1990 to 2008
$4.3M
Intramural NIH HHS Z01 ES080046
6 · The paper itself

Abstract

The inositol pyrophosphates (PP-InsPs) are a unique subgroup of intracellular signals with diverse functions, many of which can be viewed as reflecting an overarching role in metabolic homeostasis. Thus, considerable attention is paid to the enzymes that synthesize and metabolize the PP-InsPs. One of these enzyme families - the diphosphoinositol pentakisphosphate kinases (PPIP5Ks) - provides an extremely rare example of separate kinase and phosphatase activities being present within the same protein. Herein, we review the current state of structure/function insight into the PPIP5Ks, the separate specialized activities of the two metazoan PPIP5K genes, and we describe a phylogenetic analysis that places PPIP5K evolutionary origin within the Excavata, the very earliest of eukaryotes. These different aspects of PPIP5K biology are placed in the context of a single, overriding question. Why are they bifunctional: i.e., what is the particular significance of the ability to turn PP-InsP signaling on or off from two separate 'switches' in a single protein?

Indexed as

Evolution, MolecularInositol PhosphatesPhosphotransferases (Phosphate Group Acceptor)Signal TransductionAnimalsHumansdiphosphoinositol pentakisphosphate kinaseInositol PhosphatesPhosphotransferases (Phosphate Group Acceptor)

Identifiers

PMID31776069
PMCPMC9383039
OpenAlexW2983048362

What OpenQuestion holds

Textmetadata
LicenceTDM
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.