Evidence map›Paper›PMID 38964378›Full record

ArticleAutophagy2024

Prohibitins, Phb1 and Phb2, function as Atg8 receptors to support yeast mitophagy and also play a negative regulatory role in Atg32 processing.

Diana García-Chávez, Eunice Domínguez-Martín, Laura Kawasaki, Laura Ongay-Larios, Hilario Ruelas-Ramírez, Ariann E Mendoza-Martinez, Juan P Pardo, Soledad Funes, Roberto Coria

Abstract read
In one paragraph

Article in Autophagy, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Cryo-EM structure of the prohibitin complex in open conformation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. 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

9 authors.

Diana García-ChávezDepartamento de Bioquímica y Biología Estructural, Instituto de Fisiología Celular, Mexico City, México.
Eunice Domínguez-MartínNational Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD, USA.
Laura KawasakiDepartamento de Bioquímica y Biología Estructural, Instituto de Fisiología Celular, Mexico City, México.
Laura Ongay-LariosUnidad de Biología Molecular, Instituto de Fisiología Celular, Mexico City, México.
Hilario Ruelas-RamírezDepartamento de Genética Molecular, Instituto de Fisiología Celular, Mexico City, México.
Ariann E Mendoza-MartinezDepartamento de Genética Molecular, Instituto de Fisiología Celular, Mexico City, México.
Juan P PardoDepartamento de Bioquímica, Facultad de Medicina, Mexico City, México.
Soledad FunesDepartamento de Genética Molecular, Instituto de Fisiología Celular, Mexico City, México.
Roberto CoriaDepartamento de Bioquímica y Biología Estructural, Instituto de Fisiología Celular, Mexico City, México.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The prohibitins Phb1 and Phb2 assemble at the mitochondrial inner membrane to form a multi-dimeric complex. These scaffold proteins are highly conserved in eukaryotic cells, from yeast to mammals, and have been implicated in a variety of mitochondrial functions including aging, proliferation, and degenerative and metabolic diseases. In mammals, PHB2 regulates PINK1-PRKN mediated mitophagy by interacting with lipidated MAP1LC3B/LC3B. Despite their high conservation, prohibitins have not been linked to mitophagy in budding yeasts. In this study, we demonstrate that both Phb1 and Phb2 are required to sustain mitophagy in

Indexed as

Autophagy-Related Protein 8 FamilyAutophagy-Related ProteinsMitochondriaMitophagyProhibitinsRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsProtein BindingReceptors, Cytoplasmic and NuclearAtg32 protein, S cerevisiaeATG8 protein, S cerevisiaeAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsProhibitinsReceptors, Cytoplasmic and NuclearRepressor ProteinsSaccharomyces cerevisiae ProteinsAIM/LIR motifautophagyi-AAA protease (Yme1)PARLPINK1-PRKNrhomboid protease (Pcp1)

Identifiers

PMID38964378
PMCPMC11572199

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.