MétaCan
Menu
← Back to cohort
Record W4407096057 · doi:10.1016/j.jbc.2025.108253

Transmembrane Parkinson’s disease mutation of PINK1 leads to altered mitochondrial anchoring

2025· article· en· W4407096057 on OpenAlexafffund
Raelynn Brassard, Elena Arutyunova, Emmanuella Takyi, L. Michel Espinoza‐Fonseca, Howard S. Young, Nicolas Touret, M. Joanne Lemieux

Bibliographic record

VenueJournal of Biological Chemistry · 2025
Typearticle
Languageen
FieldMedicine
TopicParkinson's Disease Mechanisms and Treatments
Canadian institutionsWomen and Children’s Health Research InstituteUniversity of Alberta
FundersNational Heart, Lung, and Blood InstituteCanadian Institutes of Health ResearchNatural Sciences and Engineering Research Council of CanadaParkinson Association of AlbertaNational Institutes of HealthUniversity of AlbertaCanada Foundation for InnovationUniversity of Michigan
KeywordsPINK1LRRK2MutationMitochondrionParkinson's diseaseTransmembrane proteinCell biologyDiseaseAnchoringBiologyGeneticsChemistryParkinMedicineGeneInternal medicinePsychology

Abstract

fetched live from OpenAlex

Parkinson's disease is a devastating neurodegenerative disease resulting from the death of dopaminergic neurons in the substantia nigra pars compacta of the midbrain. Familial and sporadic forms of the disease have been linked to mitochondrial dysfunction. Pathology has been identified with mutations in the PARK6 gene encoding PTEN-induced kinase 1 (PINK1), a quality control protein in the mitochondria. Disease-associated mutations at the transmembrane (TM) region of PINK1 protein were predicted to disrupt the cleavage of the TM region by the PARL (presenilin-associated rhomboid-like) protease at the inner mitochondrial membrane. Here, using microscopy, kinetic analysis, and molecular dynamics simulations, we analyzed three Parkinson's disease-associated TM mutations; PINK1-C92F, PINK1-R98W, and PINK1-I111S, and found that mitochondrial localization and cleavage by the PARL protease were not significantly impaired. However, clearance of hydrolyzed PINK1-R98W appears to be compromised because of altered positioning of the protein in the outer mitochondrial membrane, preventing association with translocase of the outer membrane complexes and slowing cleavage by PARL. This single amino acid change slows degradation of proteolyzed PINK1, increasing its accumulation at the outer mitochondrial membrane and resulting in increased mitophagy and decreased mitochondrial content among these cells.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

How this classification was reachedexpand

Full frame machine prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. The Gemma side is a direct model label for every work in the frame, read from the title-only record. The Codex side is a classifier learned from the 10,348 direct Codex labels and calibrated to design-weighted sample rates; fields without enough sample support carry no Codex call. Candidate is the union of the two sides; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: metacan-v3-hybrid-931329e0061cValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Bench or experimental · Consensus signal: Bench or experimental
GenreCandidate signal: Empirical · Consensus signal: Empirical
Teacher disagreement score0.002
Threshold uncertainty score0.003

Distilled classifier scores by category (both heads)

CategoryCodexGemma
Metaresearch0.0000.000
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0000.000
Research integrity0.0000.000
Insufficient payload (model declined to judge)0.0010.000

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.023
GPT teacher head0.290
Teacher spread0.267 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Classification

machine, unvalidated

Machine predicted; a candidate call from one source (direct Gemma or distilled Codex), not a consensus.

The models applied no category: nothing in the taxonomy fit this work.
Study designBench or experimental
Domainnot available
GenreEmpirical

How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".

Quick stats

Citations9
Published2025
Admission routes2
Has abstractyes

Explore more

Same venueJournal of Biological Chemistry→Same topicParkinson's Disease Mechanisms and Treatments→French-language works237,207→