Evidence map›Paper›PMID 33006972›Full record

ArticlePLoS genetics2020

The O-GlcNAc transferase OGT is a conserved and essential regulator of the cellular and organismal response to hypertonic stress.

Sarel J Urso, Marcella Comly, John A Hanover, Todd Lamitina

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 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
1.5field-weighted citation impact, top 17% 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, 36 citations in OpenAlex.

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  7. Oocyte mitochondria link maternal environment to offspring phenotype.bioRxiv : the preprint server for biology · 2025
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  11. Identification of a Polypeptide Inhibitor ofJournal of the American Chemical Society · 2024
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  12. Review
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  14. Low humidity enhances thermotolerance inmicroPublication biology · 2024
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  15. Article
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  19. EndogenousmicroPublication biology · 2023
    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

4 authors at 2 institutions in 1 country.

Sarel J UrsoGraduate Program in Cell Biology and Molecular Physiology, University of Pittsburgh School of Medicine, Pittsburgh, PA, United States of America.ORCID 0000-0001-9792-0249
Marcella ComlyLaboratory of Cellular and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institute of Health, Bethesda, MD, United States of America.ORCID 0000-0001-8832-922X
John A HanoverLaboratory of Cellular and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institute of Health, Bethesda, MD, United States of America.
Todd LamitinaGraduate Program in Cell Biology and Molecular Physiology, University of Pittsburgh School of Medicine, Pittsburgh, PA, United States of America.ORCID 0000-0001-7332-9075
National Institute of Diabetes and Digestive and Kidney Diseases · USUniversity of Pittsburgh · US

Funding

Enhancing and expanding the CGC Strain CollectionP40OD010440 · OD · UNIVERSITY OF MINNESOTA · PI Ann E. Rougvie · 2012 to 2026
$7.5M
Regulation of stress-specific protein translation by the O-GlcNaC transferase ogt-1 and 3' mRNA processingR01GM135577 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI LAMITINA, SAMUEL T · 2020 to 2023
$1.5M
Bipartite regulation of cellular osmosensing in C. elegansR01GM105655 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI LAMITINA, SAMUEL T · 2014 to 2017
$1.2M
NIGMS NIH HHS R01 GM105655NIGMS NIH HHS R01 GM135577NIH HHS P40 OD010440
6 · The paper itself

Abstract

The conserved O-GlcNAc transferase OGT O-GlcNAcylates serine and threonine residues of intracellular proteins to regulate their function. OGT is required for viability in mammalian cells, but its specific roles in cellular physiology are poorly understood. Here we describe a conserved requirement for OGT in an essential aspect of cell physiology: the hypertonic stress response. Through a forward genetic screen in Caenorhabditis elegans, we discovered OGT is acutely required for osmoprotective protein expression and adaptation to hypertonic stress. Gene expression analysis shows that ogt-1 functions through a post-transcriptional mechanism. Human OGT partially rescues the C. elegans phenotypes, suggesting that the osmoregulatory functions of OGT are ancient. Intriguingly, expression of O-GlcNAcylation-deficient forms of human or worm OGT rescue the hypertonic stress response phenotype. However, expression of an OGT protein lacking the tetracopeptide repeat (TPR) domain does not rescue. Our findings are among the first to demonstrate a specific physiological role for OGT at the organismal level and demonstrate that OGT engages in important molecular functions outside of its well described roles in post-translational O-GlcNAcylation of intracellular proteins.

Indexed as

Osmotic PressureAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsGene Expression Regulation, EnzymologicHumansN-AcetylglucosaminyltransferasesProtein DomainsProtein Processing, Post-TranslationalSerineThreonineCaenorhabditis elegans ProteinsN-AcetylglucosaminyltransferasesO-GlcNAc transferaseogt-1 protein, C elegansOGT protein, humanSerineThreonine

Identifiers

PMID33006972
PMCPMC7556452
OpenAlexW3089805745

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.