Evidence map›Paper›PMID 31276588›Full record

ArticleNucleic acids research2019

Inositol pyrophosphates impact phosphate homeostasis via modulation of RNA 3' processing and transcription termination.

Ana M Sanchez, Angad Garg, Stewart Shuman, Beate Schwer

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 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
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

37 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
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  7. Enabling Technologies for the Dissection of Inositol Pyrophosphate Physiology.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
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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

4 authors at 2 institutions in 1 country.

Ana M SanchezDepartment of Microbiology and Immunology, Weill Cornell Medical College, New York, NY 10065, USA.
Angad GargMolecular Biology Program, Sloan-Kettering Institute, New York, NY 10065, USA.
Stewart ShumanMolecular Biology Program, Sloan-Kettering Institute, New York, NY 10065, USA.
Beate SchwerDepartment of Microbiology and Immunology, Weill Cornell Medical College, New York, NY 10065, USA.
Cornell University · USKettering University · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
mRNA Capping EnzymesR01GM052470 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SCHWER, BEATE, SHUMAN, STEWART H · 1995 to 2019
$9.9M
Mechanisms of DNA and RNA TransactionsR35GM126945 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI Stewart H Shuman · 2018 to 2026
$8.9M
NCI NIH HHS P30 CA008748NIGMS NIH HHS R01 GM052470NIGMS NIH HHS R35 GM126945
6 · The paper itself

Abstract

Fission yeast phosphate acquisition genes pho1, pho84, and tgp1 are repressed in phosphate-rich medium by transcription of upstream lncRNAs. Here, we show that phosphate homeostasis is subject to metabolite control by inositol pyrophosphates (IPPs), exerted through the 3'-processing/termination machinery and the Pol2 CTD code. Increasing IP8 (via Asp1 IPP pyrophosphatase mutation) de-represses the PHO regulon and leads to precocious termination of prt lncRNA synthesis. pho1 de-repression by IP8 depends on cleavage-polyadenylation factor (CPF) subunits, termination factor Rhn1, and the Thr4 letter of the CTD code. pho1 de-repression by mutation of the Ser7 CTD letter depends on IP8. Simultaneous inactivation of the Asp1 and Aps1 IPP pyrophosphatases is lethal, but this lethality is suppressed by mutations of CPF subunits Ppn1, Swd22, Ssu72, and Ctf1 and CTD mutation T4A. Failure to synthesize IP8 (via Asp1 IPP kinase mutation) results in pho1 hyper-repression. Synthetic lethality of asp1Δ with Ppn1, Swd22, and Ssu72 mutations argues that IP8 plays an important role in essential 3'-processing/termination events, albeit in a manner genetically redundant to CPF. Transcriptional profiling delineates an IPP-responsive regulon composed of genes overexpressed when IP8 levels are increased. Our results establish a novel role for IPPs in cell physiology.

Indexed as

Gene Expression Regulation, FungalRegulonTranscription Termination, GeneticAcid PhosphataseCleavage And Polyadenylation Specificity FactorCytoskeletal ProteinsGene DeletionInositol PhosphatesMembrane Transport ProteinsMultifunctional EnzymesNuclear ProteinsProtein IsoformsPyrophosphatasesRNA, Long NoncodingSchizosaccharomycesSchizosaccharomyces pombe ProteinsAcid Phosphataseacid phosphatase Pho1, S pombeaps1 protein, S pombeAsp1 protein, S pombeCleavage And Polyadenylation Specificity FactorCytoskeletal ProteinsInositol PhosphatesMembrane Transport ProteinsMultifunctional EnzymesNuclear ProteinsProtein IsoformsPyrophosphatasesRhn1 protein, S pombeRNA, Long NoncodingSchizosaccharomyces pombe ProteinsTgp1 protein, S pombe

Identifiers

PMID31276588
PMCPMC6895273
OpenAlexW2953868495

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.