Evidence map›Paper›PMID 22745122›Full record

ArticleThe Journal of biological chemistry2012

Modulation of dynamin-related protein 1 (DRP1) function by increased O-linked-β-N-acetylglucosamine modification (O-GlcNAc) in cardiac myocytes.

Thomas Gawlowski, Jorge Suarez, Brian Scott, Moises Torres-Gonzalez, Hong Wang, Raphaela Schwappacher, Xuemei Han, John R Yates, Masahiko Hoshijima, Wolfgang Dillmann

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 148 papers.

0numbers the graph read from it
0cells of the map it votes in
148citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

148 citing papers in PubMed, 193 citations in OpenAlex.

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  11. Conformational Rearrangement of Fission DSPs.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  12. Article
  13. Article
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  18. Coupling of glucose metabolism with mitophagy via O-GlcNAcylation of PINK1.International journal of biological sciences · 2025
    Article
  19. Improving metabolic support during normothermicFrontiers in cardiovascular medicine · 2025
    Review
  20. Review

88 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Thomas GawlowskiDepartment of Medicine, University of California, San Diego, La Jolla, CA 92039, USA.
Jorge Suarez
Brian Scott
Moises Torres-Gonzalez
Hong Wang
Raphaela Schwappacher
Xuemei Han
John R Yates
Masahiko Hoshijima
Wolfgang Dillmann
University of California, San Diego · USScripps Research Institute · US

Funding

ZDS2P REGULATES SWE1P-DEPENDENT POLARIZED CELL GROWTH IN S CEREVISIAEP41RR011823 · NCRR · UNIVERSITY OF WASHINGTON · PI FIELDS, STANLEY · 1996 to 2011
$24.7M
TrainingP41GM103533 · NIGMS · UNIVERSITY OF WASHINGTON · PI YATES III, JOHN R · 2012 to 2021
$20.7M
San Diego EXPORT Comprehensive NCMHD Research CenterP60MD000220 · NIMHD · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI VILLARREAL, FRANCISCO · 2002 to 2011
$11.0M
U of Calif, San Diego Neuroscience Microscopy ImagingP30NS047101 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GLEESON, JOSEPH G, ZHENG, BINHAI · 2003 to 2022
$9.0M
DIABETIC CARDIOMYOPATHY AND CALCIUM FLUXR01HL066917 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI DILLMANN, WOLFGANG H · 2000 to 2011
$4.8M
NCRR NIH HHS P41 RR011823NHLBI NIH HHS 3R01HL066917-10S1NHLBI NIH HHS HL066917NHLBI NIH HHS R01 HL066917NIGMS NIH HHS P41 GM103533NIMHD NIH HHS P60 MD000220NIMHD NIH HHS P60 MD00220NINDS NIH HHS P30 NS047101
6 · The paper itself

Abstract

O-linked-N-acetyl-glucosamine glycosylation (O-GlcNAcylation) of the serine and threonine residues of cellular proteins is a dynamic process and affects phosphorylation. Prolonged O-GlcNAcylation has been linked to diabetes-related complications, including mitochondrial dysfunction. Mitochondria are dynamically remodeling organelles, that constantly fuse (fusion) and divide (fission). An imbalance of this process affects mitochondrial function. In this study, we found that dynamin-related protein 1 (DRP1) is O-GlcNAcylated in cardiomyocytes at threonine 585 and 586. O-GlcNAcylation was significantly enhanced by the chemical inhibition of N-acetyl-glucosaminidase. Increased O-GlcNAcylation decreases the phosphorylation of DRP1 at serine 637, which is known to regulate DRP1 function. In fact, increased O-GlcNAcylation augments the level of the GTP-bound active form of DRP1 and induces translocation of DRP1 from the cytoplasm to mitochondria. Mitochondrial fragmentation and decreased mitochondrial membrane potential also accompany the increased O-GlcNAcylation. In conclusion, this report shows, for the first time, that O-GlcNAcylation modulates DRP1 functionality in cardiac muscle cells.

Indexed as

AcetylationAcetylglucosamineAcetylglucosaminidaseAnimalsCytoplasmDiabetes ComplicationsDiabetes Mellitus, ExperimentalDynaminsHumansMembrane Potential, MitochondrialMiceMitochondria, HeartMitochondrial DiseasesMuscle ProteinsMyocytes, CardiacPhosphorylationAcetylglucosamineAcetylglucosaminidaseDnm1l protein, mouseDynaminsMuscle Proteins

Identifiers

PMID22745122
PMCPMC3436129
OpenAlexW2044370075

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.