Evidence map›Paper›PMID 26828065›Full record

ArticleThe Journal of biological chemistry2016

A Novel Inositol Pyrophosphate Phosphatase in Saccharomyces cerevisiae: Siw14 PROTEIN SELECTIVELY CLEAVES THE β-PHOSPHATE FROM 5-DIPHOSPHOINOSITOL PENTAKISPHOSPHATE (5PP-IP5).

Elizabeth A Steidle, Lucy S Chong, Mingxuan Wu, Elliott Crooke, Dorothea Fiedler, Adam C Resnick, Ronda J Rolfes

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

46 citing papers in PubMed, 70 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Evolution of cross-tolerance to metals in yeast.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  8. Anti-Prion Systems in Saccharomyces cerevisiae.Journal of neurochemistry · 2025
    Review
  9. Article
  10. Article
  11. Increased CONature communications · 2024
    Article
  12. Review
  13. Review
  14. Prions in Microbes: The Least in the Most.Journal of microbiology (Seoul, Korea) · 2023
    Review
  15. Article
  16. Article
  17. Anti-Prion Systems inViruses · 2022
    Review
  18. Review
  19. Biochemistry · 2022
    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

7 authors at 3 institutions in 1 country.

Elizabeth A SteidleFrom the Department of Biology, Georgetown University, Washington, D. C. 20057.
Lucy S Chongthe Division of Neurosurgery, Children's Hospital of Philadelphia, Philadelphia, Pennsylvania 19104.
Mingxuan Wuthe Department of Chemistry, Princeton University, Princeton, New Jersey 08544, and.
Elliott Crookethe Department of Biochemistry and Molecular and Cellular Biology, Georgetown University, Washington, D. C. 20057.
Dorothea Fiedlerthe Department of Chemistry, Princeton University, Princeton, New Jersey 08544, and.
Adam C Resnickthe Division of Neurosurgery, Children's Hospital of Philadelphia, Philadelphia, Pennsylvania 19104, resnick@email.chop.edu.
Ronda J RolfesFrom the Department of Biology, Georgetown University, Washington, D. C. 20057, rolfesr@georgetown.edu.
Georgetown University · USChildren's Hospital of Philadelphia · USPrinceton University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inositol pyrophosphates are high energy signaling molecules involved in cellular processes, such as energetic metabolism, telomere maintenance, stress responses, and vesicle trafficking, and can mediate protein phosphorylation. Although the inositol kinases underlying inositol pyrophosphate biosynthesis are well characterized, the phosphatases that selectively regulate their cellular pools are not fully described. The diphosphoinositol phosphate phosphohydrolase enzymes of the Nudix protein family have been demonstrated to dephosphorylate inositol pyrophosphates; however, theSaccharomyces cerevisiaehomolog Ddp1 prefers inorganic polyphosphate over inositol pyrophosphates. We identified a novel phosphatase of the recently discovered atypical dual specificity phosphatase family as a physiological inositol pyrophosphate phosphatase. Purified recombinant Siw14 hydrolyzes the β-phosphate from 5-diphosphoinositol pentakisphosphate (5PP-IP5or IP7)in vitro. In vivo,siw14Δ yeast mutants possess increased IP7levels, whereas heterologousSIW14overexpression eliminates IP7from cells. IP7levels increased proportionately whensiw14Δ was combined withddp1Δ orvip1Δ, indicating independent activity by the enzymes encoded by these genes. We conclude that Siw14 is a physiological phosphatase that modulates inositol pyrophosphate metabolism by dephosphorylating the IP7isoform 5PP-IP5to IP6.

Indexed as

Gene Expression Regulation, FungalCloning, MolecularEscherichia coliGene DeletionGenetic Complementation TestInositol PhosphatesKineticsPhosphotransferases (Phosphate Group Acceptor)Protein Tyrosine PhosphatasesRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionSubstrate Specificity1-diphosphoinositol pentakisphosphateinositol hexakisphosphate kinaseInositol PhosphatesPhosphotransferases (Phosphate Group Acceptor)Protein Tyrosine PhosphatasesRecombinant ProteinsSaccharomyces cerevisiae ProteinsSiw14 protein, S cerevisiaedual-specificity phosphoprotein phosphataseinositol phosphateIP7phosphatasephosphatidylinositolSaccharomyces cerevisiaesecond messengerSiw14Vip1

Identifiers

PMID26828065
PMCPMC4807264
OpenAlexW2291775309

What OpenQuestion 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 OpenQuestion graph.