Evidence map›Paper›PMID 21115803›Full record

ArticleThe Journal of cell biology2010

Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL.

Seok Min Jin, Michael Lazarou, Chunxin Wang, Lesley A Kane, Derek P Narendra, Richard J Youle

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 774 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
774citing papers in PubMed, 2 pooled it
30.6field-weighted citation impact, top 1% 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

774 citing papers in PubMed, 2 syntheses or guidelines pooled it, 1,323 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Regulation and roles of mammalian mitophagy.Nature reviews. Molecular cell biology · 2026
    Review
  4. Article
  5. Regulation of cellular proteostasis via mitochondrial protein import.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  6. Article
  7. Mitochondrial depolarization stabilizes the vitamin BProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Article

714 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

6 authors at 3 institutions in 2 countries.

Seok Min JinBiochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.
Michael Lazarou
Chunxin Wang
Lesley A Kane
Derek P Narendra
Richard J Youle
National Institutes of Health · USMRC Mitochondrial Biology Unit · GBNational Institute of Neurological Disorders and Stroke · US

Funding

Role of mitochondria in neurodegenerative diseasesZIANS003123 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI YOULE, RICHARD JAMES · 2011 to 2025
$28.8M
Intramural NIH HHS
6 · The paper itself

Abstract

PINK1 is a mitochondrial kinase mutated in some familial cases of Parkinson's disease. It has been found to work in the same pathway as the E3 ligase Parkin in the maintenance of flight muscles and dopaminergic neurons in Drosophila melanogaster and to recruit cytosolic Parkin to mitochondria to mediate mitophagy in mammalian cells. Although PINK1 has a predicted mitochondrial import sequence, its cellular and submitochondrial localization remains unclear in part because it is rapidly degraded. In this study, we report that the mitochondrial inner membrane rhomboid protease presenilin-associated rhomboid-like protein (PARL) mediates cleavage of PINK1 dependent on mitochondrial membrane potential. In the absence of PARL, the constitutive degradation of PINK1 is inhibited, stabilizing a 60-kD form inside mitochondria. When mitochondrial membrane potential is dissipated, PINK1 accumulates as a 63-kD full-length form on the outer mitochondrial membrane, where it can recruit Parkin to impaired mitochondria. Thus, differential localization to the inner and outer mitochondrial membranes appears to regulate PINK1 stability and function.

Indexed as

Membrane Potential, MitochondrialAnimalsHeLa CellsHumansMetalloproteasesMiceMitochondrial ProteinsProtein KinasesPTEN-Induced Putative KinaseRNA, Small InterferingTransfectionMetalloproteasesMitochondrial ProteinsProtein KinasesPTEN-Induced Putative KinaseRNA, Small Interfering

Identifiers

PMID21115803
PMCPMC2995166
OpenAlexW2038834667

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.