Evidence map›Paper›PMID 19762472›Full record

ArticleThe Journal of biological chemistry2009

Mitochondrial localization of PARP-1 requires interaction with mitofilin and is involved in the maintenance of mitochondrial DNA integrity.

Marianna N Rossi, Mariarosaria Carbone, Cassandra Mostocotto, Carmine Mancone, Marco Tripodi, Rossella Maione, Paolo Amati

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

87 citing papers in PubMed, 159 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Mitochondrial PARP1 regulates NADExperimental & molecular medicine · 2022
    Article
  10. Review
  11. Mitochondrial DNA Instability in Mammalian Cells.Antioxidants & redox signaling · 2022
    Review
  12. Article
  13. Review
  14. Instability in NADeLife · 2021
    Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Mitochondrial NADMolecular cell · 2021
    Article
  20. The Mitochondrial Response to DNA Damage.Frontiers in cell and developmental biology · 2021
    Review

27 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

7 authors at 2 institutions in 1 country.

Marianna N RossiPasteur Institute-Fondazione Cenci Bolognetti, Department of Cellular Biotechnologies and Hematology, University of Rome La Sapienza, Viale Regina Elena 324, 00161 Rome, Italy.
Mariarosaria Carbone
Cassandra Mostocotto
Carmine Mancone
Marco Tripodi
Rossella Maione
Paolo Amati
Istituto Pasteur · ITIstituti di Ricovero e Cura a Carattere Scientifico · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Poly(ADP-ribose)polymerase-1 (PARP-1) is a predominantly nuclear enzyme that exerts numerous functions in cellular physiology and pathology, from maintenance of DNA stability to transcriptional regulation. Through a proteomic analysis of PARP-1 co-immunoprecipitation complexes, we identified Mitofilin, a mitochondrial protein, as a new PARP-1 interactor. This result prompted us to further investigate the presence and the role of the enzyme in mitochondria. Using laser confocal microscopy and Western blot analysis of purified mitochondria, we demonstrated the mitochondrial localization of a fraction of PARP-1. Further, the effects of overexpressing or down-regulating Mitofilin showed that this protein promotes and is required for PARP-1 mitochondrial localization. We also report several lines of evidence suggesting that intramitochondrial PARP-1 plays a role in mitochondrial DNA (mtDNA) damage signaling and/or repair. First, we show that PARP-1 binds to different regions throughout the mtDNA. Moreover, we demonstrated that the depletion of either PARP-1 or Mitofilin, which abrogates the mitochondrial localization of the enzyme, leads to the accumulation of mtDNA damage. Finally, we show that DNA ligase III, known to be required for mtDNA repair, participates in a PARP-1-containing complex bound to mtDNA. This work highlights a new environment for PARP-1, opening the possibility that at least some of the nuclear functions of the enzyme can be also extended to mtDNA metabolism.

Indexed as

Blotting, WesternChromatin ImmunoprecipitationDNA Ligase ATPDNA LigasesDNA, MitochondrialFibroblastsHeLa CellsHumansImmunoprecipitationMass SpectrometryMicroscopy, ConfocalMitochondriaMitochondrial ProteinsMuscle ProteinsPoly-ADP-Ribose Binding ProteinsPoly (ADP-Ribose) Polymerase-1DNA Ligase ATPDNA ligase III alpha protein, XenopusDNA LigasesDNA, MitochondrialIMMT protein, humanLIG3 protein, humanMitochondrial ProteinsMuscle ProteinsPARP1 protein, humanPoly-ADP-Ribose Binding ProteinsPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) Polymerase InhibitorsPoly(ADP-ribose) PolymerasesRNA, Small InterferingXenopus Proteins

Identifiers

PMID19762472
PMCPMC2797232
OpenAlexW1964867682

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.