Evidence map›Paper›PMID 42258734›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2026

Alpha-synuclein fibrils induce budding of mitochondrial-derived vesicles.

Thomas Braun, Viviane Reber, Cinzia Tiberi, Andri Fränkl, Dhiman Ghosh, Roland Riek, Tetiana Serdiuk

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Alpha-synuclein fibrils induce budding of mitochondrial-derived vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2026
    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

7 authors.

Thomas BraunBiozentrum, University of Basel, Basel 4056, Switzerland.ORCID 0000-0002-9148-0200
Viviane ReberDepartment of Biology, Institute of Molecular Systems Biology, Swiss Federal Institute of Technology Zürich, Zürich 8093, Switzerland.ORCID 0000-0001-7653-6918
Cinzia TiberiBioEM Lab, Biozentrum, University of Basel, Basel 4058, Switzerland.
Andri FränklBiozentrum, University of Basel, Basel 4056, Switzerland.
Dhiman GhoshDepartment of Chemistry and Applied Biosciences, Institute of Molecular Physical Science, Swiss Federal Institute of Technology Zürich, Zürich 8093, Switzerland.
Roland RiekDepartment of Chemistry and Applied Biosciences, Institute of Molecular Physical Science, Swiss Federal Institute of Technology Zürich, Zürich 8093, Switzerland.ORCID 0000-0002-6333-066X
Tetiana SerdiukDepartment of Biology, Institute of Molecular Systems Biology, Swiss Federal Institute of Technology Zürich, Zürich 8093, Switzerland.ORCID 0000-0002-3706-5911

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-synuclein (α-syn) aggregation is a hallmark of synucleinopathies, a class of neurodegenerative disorders such as Parkinson's disease (PD). Several lines of evidence indicate the involvement of mitochondria in the disease pathology. Despite extensive study, the link between α-syn aggregation and mechanisms of mitochondrial toxicity remains not fully understood. Using high-resolution imaging with electron microscopy, we examined SH-SY5Y cells exposed to α-syn fibrils vs control cells with a focus on mitochondria. We found that upon exposure to α-syn fibrils, mitochondria cristae structure gets defects, and mitochondria enhance the budding of mitochondrial-derived vesicles (MDVs). MDV formation reflects an evolutionarily conserved mechanism reminiscent of bacterial outer membrane vesicle biogenesis. Structural proteomics analysis by mass spectrometry corroborates this microscopy observation by identifying changes in multiple proteins that regulate cristae structure, MDV formation, and trafficking. Our results suggest that α-syn may promote MDV generation, and support an important link between α-syn and mitochondria which will be important for future mechanistic studies. The processes we detected could be of interest for diagnostics and potential therapeutic interventions.

Indexed as

alpha-SynucleinMitochondriaCell Line, TumorHumansMitochondrial MembranesProteomicsalpha-Synuclein

Identifiers

PMID42258734
PMCPMC13273258

What Socratic holds

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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 Socratic graph.