Evidence map›Paper›PMID 34764359›Full record

ArticleScientific reports2021

Blocked O-GlcNAc cycling alters mitochondrial morphology, function, and mass.

Elizabeth O Akinbiyi, Lara K Abramowitz, Brianna L Bauer, Maria S K Stoll, Charles L Hoppel, Chao-Pin Hsiao, John A Hanover, Jason A Mears

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

29 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Conformational Rearrangement of Fission DSPs.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  8. Article
  9. Article
  10. Coupling of glucose metabolism with mitophagy via O-GlcNAcylation of PINK1.International journal of biological sciences · 2025
    Article
  11. Review
  12. Article
  13. Review
  14. O-GlcNAcylation mediates HActa pharmacologica Sinica · 2024
    Article
  15. Article
  16. Article
  17. O-GlcNAcylation in ischemic diseases.Frontiers in pharmacology · 2024
    Review
  18. Review
  19. Review
  20. Review
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

8 authors at 3 institutions in 1 country.

Elizabeth O AkinbiyiDepartment of Pathology, Case Western Reserve University School of Medicine, Cleveland, OH, 44106, USA.
Lara K AbramowitzLaboratory of Cellular and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892, USA.
Brianna L BauerDepartment of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, OH, 44106, USA.
Maria S K StollCenter for Mitochondrial Diseases, Case Western Reserve University School of Medicine, Cleveland, OH, 44106, USA.
Charles L HoppelDepartment of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, OH, 44106, USA.
Chao-Pin HsiaoCenter for Mitochondrial Diseases, Case Western Reserve University School of Medicine, Cleveland, OH, 44106, USA.
John A HanoverLaboratory of Cellular and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892, USA.
Jason A MearsDepartment of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, OH, 44106, USA. jason.mears@case.edu.
Case Western Reserve University · USNational Institute of Diabetes and Digestive and Kidney Diseases · USUniversity School · US

Funding

PREDOCTORAL TRAINING PROGRAM IN MOLECULAR THERAPEUTICST32GM008803 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI MIEYAL, JOHN J, NIEMAN, MARVIN THOMAS · 2001 to 2023
$4.2M
Immunology Training Program-PredoctoralT32AI089474 · NIAID · CASE WESTERN RESERVE UNIVERSITY · PI COBB, BRIAN A · 2010 to 2025
$3.4M
Supplement: Defining Molecular Interactions that Drive Mitochondrial FissionR01GM125844 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI Jason Mears · 2018 to 2026
$2.8M
Mitochondrial Dynamics in Brain TumorInitiating CellsR01CA208516 · NCI · CASE WESTERN RESERVE UNIVERSITY · PI MEARS, JASON · 2017 to 2021
$1.6M
Acquisition of a Leica TCS SP5 Confocal Microscope For A Multi-User FacilityS10OD016164 · OD · CASE WESTERN RESERVE UNIVERSITY · PI CONRAD, PATRICIA A · 2013 to 2013
$597k
NCI NIH HHS CA208516NCI NIH HHS R01 CA208516NIAID NIH HHS T32 AI089474NIGMS NIH HHS GM125844NIGMS NIH HHS R01 GM125844NIGMS NIH HHS T32 GM008803NIH HHS S10 OD016164
6 · The paper itself

Abstract

O-GlcNAcylation is a prevalent form of glycosylation that regulates proteins within the cytosol, nucleus, and mitochondria. The O-GlcNAc modification can affect protein cellular localization, function, and signaling interactions. The specific impact of O-GlcNAcylation on mitochondrial morphology and function has been elusive. In this manuscript, the role of O-GlcNAcylation on mitochondrial fission, oxidative phosphorylation (Oxphos), and the activity of electron transport chain (ETC) complexes were evaluated. In a cellular environment with hyper O-GlcNAcylation due to the deletion of O-GlcNAcase (OGA), mitochondria showed a dramatic reduction in size and a corresponding increase in number and total mitochondrial mass. Because of the increased mitochondrial content, OGA knockout cells exhibited comparable coupled mitochondrial Oxphos and ATP levels when compared to WT cells. However, we observed reduced protein levels for complex I and II when comparing normalized mitochondrial content and reduced linked activity for complexes I and III when examining individual ETC complex activities. In assessing mitochondrial fission, we observed increased amounts of O-GlcNAcylated dynamin-related protein 1 (Drp1) in cells genetically null for OGA and in glioblastoma cells. Individual regions of Drp1 were evaluated for O-GlcNAc modifications, and we found that this post-translational modification (PTM) was not limited to the previously characterized residues in the variable domain (VD). Additional modification sites are predicted in the GTPase domain, which may influence enzyme activity. Collectively, these results highlight the impact of O-GlcNAcylation on mitochondrial dynamics and ETC function and mimic the changes that may occur during glucose toxicity from hyperglycemia.

Indexed as

AcylationAnimalsCell LineCell Line, TumorDynaminsGlucoseGlycosylationHCT116 CellsHumansMiceMice, KnockoutMitochondria, HeartMitochondrial DynamicsMultienzyme ComplexesN-AcetylglucosaminyltransferasesOxidative PhosphorylationDynaminsGlucoseMultienzyme ComplexesN-Acetylglucosaminyltransferases

Identifiers

PMID34764359
PMCPMC8586252
OpenAlexW3212431784

What OpenQuestion holds

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Registered trials

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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.