Evidence map›Paper›PMID 25060553›Full record

ArticleCell death and differentiation2015

Transglutaminase 2 ablation leads to mitophagy impairment associated with a metabolic shift towards aerobic glycolysis.

F Rossin, M D'Eletto, L Falasca, S Sepe, S Cocco, G M Fimia, M Campanella, P G Mastroberardino, M G Farrace, M Piacentini

Open access · bronzeAbstract read
In one paragraph

Article in Cell death and differentiation, 2015. 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
4.6field-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

29 citing papers in PubMed, 55 citations in OpenAlex.

  1. Review
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  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. The Key Role of Mitochondrial Function in Health and Disease.Antioxidants (Basel, Switzerland) · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Glycolysis regulated transglutaminase 2 activation in cardiopulmonary fibrogenic remodeling.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  18. Article
  19. Review
  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

10 authors at 5 institutions in 3 countries.

F RossinDepartment of Biology, University of Rome 'Tor Vergata', Rome, Italy.
M D'ElettoDepartment of Biology, University of Rome 'Tor Vergata', Rome, Italy.
L FalascaNational Institute for Infectious Diseases I.R.C.C.S. 'L. Spallanzani', Rome, Italy.
S SepeDepartment of Genetics, Erasmus Medical Center, Rotterdam, The Netherlands.
S CoccoEuropean Brain Research Institute (EBRI), Rita Levi-Montalcini Foundation, Rome, Italy.
G M Fimia1] National Institute for Infectious Diseases I.R.C.C.S. 'L. Spallanzani', Rome, Italy [2] Department of Biological and Environmental Sciences and Technologies (DiSTeBA), University of Salento, Lecce, Italy.
M Campanella1] European Brain Research Institute (EBRI), Rita Levi-Montalcini Foundation, Rome, Italy [2] Department of Comparative Biomedical Sciences, Royal Veterinary College, University of London and UCL Consortium for Mitochondrial Research (CfMR), London, UK.
P G MastroberardinoDepartment of Genetics, Erasmus Medical Center, Rotterdam, The Netherlands.
M G FarraceDepartment of Biology, University of Rome 'Tor Vergata', Rome, Italy.
M Piacentini1] Department of Biology, University of Rome 'Tor Vergata', Rome, Italy [2] National Institute for Infectious Diseases I.R.C.C.S. 'L. Spallanzani', Rome, Italy.
University of Rome Tor Vergata · ITErasmus MC · NLEuropean Brain Research Institute · ITIstituto Nazionale per le Malattie Infettive Lazzaro Spallanzani · ITRoyal Veterinary College · GB

Funding

Biotechnology and Biological Sciences Research Council BB/I013695/1
6 · The paper itself

Abstract

Macroautophagy selectively degrades dysfunctional mitochondria by a process known as mitophagy. Here we demonstrate the involvement of transglutaminase 2 (TG2) in the turnover and degradation of damaged mitochondria. In TG2-ablated cells we observed the presence of a large number of fragmented mitochondria that display decreased membrane potential, downregulation of IF1 along with increased Drp1 and PINK1 levels, two key proteins regulating the mitochondrial fission. Of note, we demonstrate that in healthy mitochondria, TG2 interacts with the dynamic proteins Drp1 and Fis1; interestingly, their interaction is largely reduced upon induction of the fission process by carbonyl cyanide m-chlorophenyl hydrazine (CCCP). In keeping with these findings, mitochondria lacking TG2 are more susceptible to CCCP treatment. As a consequence of accumulation of damaged mitochondria, cells lacking TG2 increased their aerobic glycolysis and became sensitive to the glycolytic inhibitor 2-deoxy-D-glucose (2-DG). In contrast, TG2-proficient cells are more resistant to 2-DG-induced apoptosis as the caspase 3 is inactivated through the enzyme's crosslinking activity. The data presented in this study show that TG2 plays a key role in cellular dynamics and consequently influences the energetic metabolism.

Indexed as

AerobiosisAnimalsAutophagyEnergy MetabolismGlycolysisGTP-Binding ProteinsHEK293 CellsHumansMiceMice, KnockoutMitochondriaProtein Glutamine gamma Glutamyltransferase 2TransglutaminasesGTP-Binding ProteinsProtein Glutamine gamma Glutamyltransferase 2Transglutaminases

Identifiers

PMID25060553
PMCPMC4326569
OpenAlexW2066979461

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.