Evidence map›Paper›PMID 36192422›Full record

ArticleNature communications2022

Allosteric regulation of glycogen breakdown by the second messenger cyclic di-GMP.

Maria A Schumacher, Mirka E Wörmann, Max Henderson, Raul Salinas, Andreas Latoscha, Mahmoud M Al-Bassam, Kumar Siddharth Singh, Elaine Barclay, Katrin Gunka, Natalia Tschowri

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

22 citing papers in PubMed, 28 citations in OpenAlex.

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  13. The activation ofPlant direct · 2024
    Article
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  16. Characterization of glycogen-related glycoside hydrolaseFrontiers in cellular and infection microbiology · 2024
    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

10 authors at 6 institutions in 3 countries.

Maria A Schumacher *Department of Biochemistry, Duke University School of Medicine, Durham, NC, 27710, USA. maria.schumacher@duke.edu.ORCID 0000-0002-5264-1120
Mirka E Wörmann *Institute for Biology/Microbiology, Humboldt-Universität zu Berlin, 10115, Berlin, Germany.
Max HendersonDepartment of Biochemistry, Duke University School of Medicine, Durham, NC, 27710, USA.
Raul SalinasDepartment of Biochemistry, Duke University School of Medicine, Durham, NC, 27710, USA.
Andreas LatoschaInstitute for Biology/Microbiology, Humboldt-Universität zu Berlin, 10115, Berlin, Germany.ORCID 0000-0002-3325-3819
Mahmoud M Al-BassamDepartment of Pediatrics, University of California, San Diego, La Jolla, CA, 92093, USA.
Kumar Siddharth SinghInstitute of Microbiology, Leibniz Universität Hannover, 30419, Hannover, Germany.
Elaine BarclayDepartment of Cell and Developmental Biology, John Innes Centre, Norwich, NR4 7UH, UK.
Katrin GunkaInstitute of Microbiology, Leibniz Universität Hannover, 30419, Hannover, Germany.
Natalia TschowriInstitute of Microbiology, Leibniz Universität Hannover, 30419, Hannover, Germany. tschowri@ifmb.uni-hannover.de.ORCID 0000-0002-4304-1860
Duke University · USLeibniz University Hannover · DEFederal Institute for Risk Assessment · DEHumboldt-Universität zu Berlin · DEJohn Innes Centre · GBUniversity of California San Diego · US

Funding

User Training and OutreachP30GM124169 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI PAUL David ADAMS, Gregory L Hura · 2017 to 2026
$28.6M
Deciphering fundamental biological processes involving protein-nucleic acid interactions at the molecular levelR35GM130290 · NIGMS · DUKE UNIVERSITY · PI Maria Schumacher · 2019 to 2026
$4.9M
NIGMS NIH HHS P30 GM124169NIGMS NIH HHS R35 GM130290
6 · The paper itself

Abstract

Streptomyces are our principal source of antibiotics, which they generate concomitant with a complex developmental transition from vegetative hyphae to spores. c-di-GMP acts as a linchpin in this transition by binding and regulating the key developmental regulators, BldD and WhiG. Here we show that c-di-GMP also binds the glycogen-debranching-enzyme, GlgX, uncovering a direct link between c-di-GMP and glycogen metabolism in bacteria. Further, we show c-di-GMP binding is required for GlgX activity. We describe structures of apo and c-di-GMP-bound GlgX and, strikingly, their comparison shows c-di-GMP induces long-range conformational changes, reorganizing the catalytic pocket to an active state. Glycogen is an important glucose storage compound that enables animals to cope with starvation and stress. Our in vivo studies reveal the important biological role of GlgX in Streptomyces glucose availability control. Overall, we identify a function of c-di-GMP in controlling energy storage metabolism in bacteria, which is widespread in Actinobacteria.

Indexed as

Gene Expression Regulation, BacterialStreptomycesAllosteric RegulationAnimalsAnti-Bacterial AgentsBacterial ProteinsCyclic GMPGlucoseGlycogenSecond Messenger SystemsAnti-Bacterial AgentsBacterial Proteinsbis(3',5')-cyclic diguanylic acidCyclic GMPGlucoseGlycogen

Identifiers

PMID36192422
PMCPMC9530166
OpenAlexW4300860934

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.