Evidence map›Paper›PMID 39420095›Full record

ArticleThe EMBO journal2024

Autophagy adaptors mediate Parkin-dependent mitophagy by forming sheet-like liquid condensates.

Zi Yang, Saori R Yoshii, Yuji Sakai, Jing Zhang, Haruka Chino, Roland L Knorr, Noboru Mizushima

Abstract read
In one paragraph

Article in The EMBO journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Regulation and roles of mammalian mitophagy.Nature reviews. Molecular cell biology · 2026
    Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. The Human Autophagy Core Complexes.Annual review of biochemistry · 2026
    Review
  10. Article
  11. Review
  12. Article
  13. Core principles of autophagy initiation mechanisms.Nature structural & molecular biology · 2026
    Review
  14. Article
  15. Molecular biology of the cell · 2026
    Article
  16. Review
  17. miRNA family miR-29 inhibits PINK1-PRKN signaling via ATG9A.Molecular neurodegeneration advances · 2026
    Article
  18. Review
  19. Review
  20. Review
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.

Zi YangDepartment of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
Saori R YoshiiDepartment of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
Yuji SakaiDepartment of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.ORCID http://orcid.org/0000-0002-2184-4304
Jing ZhangDepartment of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
Haruka ChinoDepartment of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
Roland L KnorrDepartment of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
Noboru MizushimaDepartment of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan. nmizu@m.u-tokyo.ac.jp.ORCID http://orcid.org/0000-0002-6258-6444

Funding

Deutsche Forschungsgemeinschaft (DFG) 460056461MEXT | Japan Society for the Promotion of Science (JSPS) 22H04919MEXT | Japan Society for the Promotion of Science (JSPS) 23K05715MEXT | JST | Exploratory Research for Advanced Technology (ERATO) JPMJER1702
6 · The paper itself

Abstract

During PINK1- and Parkin-mediated mitophagy, autophagy adaptors are recruited to damaged mitochondria to promote their selective degradation. Autophagy adaptors such as optineurin (OPTN) and NDP52 facilitate mitophagy by recruiting the autophagy-initiation machinery, and assisting engulfment of damaged mitochondria through binding to ubiquitinated mitochondrial proteins and autophagosomal ATG8 family proteins. Here, we demonstrate that OPTN and NDP52 form sheet-like phase-separated condensates with liquid-like properties on the surface of ubiquitinated mitochondria. The dynamic and liquid-like nature of OPTN condensates is important for mitophagy activity, because reducing the fluidity of OPTN-ubiquitin condensates suppresses the recruitment of ATG9 vesicles and impairs mitophagy. Based on these results, we propose a dynamic liquid-like, rather than a stoichiometric, model of autophagy adaptors to explain the interactions between autophagic membranes (i.e., ATG9 vesicles and isolation membranes) and mitochondrial membranes during Parkin-mediated mitophagy. This model underscores the importance of liquid-liquid phase separation in facilitating membrane-membrane contacts, likely through the generation of capillary forces.

Indexed as

Autophagy-Related ProteinsCell Cycle ProteinsMembrane Transport ProteinsMitochondriaMitophagyTranscription Factor TFIIIAUbiquitin-Protein LigasesAutophagyAutophagy-Related Protein 8 FamilyHeLa CellsHumansMembrane ProteinsNuclear ProteinsVesicular Transport ProteinsATG9A protein, humanAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsCALCOCO2 protein, humanCell Cycle ProteinsMembrane ProteinsMembrane Transport ProteinsNuclear ProteinsOPTN protein, humanparkin proteinTranscription Factor TFIIIAUbiquitin-Protein LigasesVesicular Transport ProteinsAutophagyLiquid–Liquid Phase SeparationMitophagyOptineurinWetting

Identifiers

PMID39420095
PMCPMC11574277

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.