Evidence map›Paper›PMID 33317697›Full record

ArticleeLife2020

Association and dissociation between the mitochondrial Far complex and Atg32 regulate mitophagy.

Aleksei Innokentev, Kentaro Furukawa, Tomoyuki Fukuda, Tetsu Saigusa, Keiichi Inoue, Shun-Ichi Yamashita, Tomotake Kanki

Open access · goldAbstract readComparative Study
In one paragraph

Article in eLife, 2020. 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
1.7field-weighted citation impact, top 14% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Mitophagy: a novel avenue for herbal medicines alleviating myocardial ischemia/reperfusion injury.Apoptosis : an international journal on programmed cell death · 2025
    Review
  2. Article
  3. Article
  4. STRIPAK, a fundamental signaling hub of eukaryotic development.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Aleksei Innokentev *Department of Cellular Physiology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.
Kentaro Furukawa *Department of Cellular Physiology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.ORCID 0000-0002-1551-1538
Tomoyuki FukudaDepartment of Cellular Physiology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.ORCID 0000-0003-2069-7127
Tetsu SaigusaDepartment of Cellular Physiology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.
Keiichi InoueDepartment of Cellular Physiology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.
Shun-Ichi YamashitaDepartment of Cellular Physiology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.
Tomotake KankiDepartment of Cellular Physiology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.ORCID 0000-0001-9646-5379
Niigata University · JP

Funding

Japan Agency for Medical Research and Development JP18gm6110013h0001Japan Society for the Promotion of Science 17H03671Japan Society for the Promotion of Science 18H04691Japan Society for the Promotion of Science 18H04858Japan Society for the Promotion of Science 18K06129Japan Society for the Promotion of Science 19H05712Japan Society for the Promotion of Science 19K22419Niigata University Kyowakai Medical Research Grant
6 · The paper itself

Abstract

Mitophagy plays an important role in mitochondrial homeostasis. In yeast, the phosphorylation of the mitophagy receptor Atg32 by casein kinase 2 is essential for mitophagy. This phosphorylation is counteracted by the yeast equivalent of the STRIPAK complex consisting of the PP2A-like protein phosphatase Ppg1 and Far3-7-8-9-10-11 (Far complex), but the underlying mechanism remains elusive. Here we show that two subpopulations of the Far complex reside in the mitochondria and endoplasmic reticulum, respectively, and play distinct roles; the former inhibits mitophagy via Atg32 dephosphorylation, and the latter regulates TORC2 signaling. Ppg1 and Far11 form a subcomplex, and Ppg1 activity is required for the assembling integrity of Ppg1-Far11-Far8. The Far complex preferentially interacts with phosphorylated Atg32, and this interaction is weakened by mitophagy induction. Furthermore, the artificial tethering of Far8 to Atg32 prevents mitophagy. Taken together, the Ppg1-mediated Far complex formation and its dissociation from Atg32 are crucial for mitophagy regulation.

Indexed as

MitophagyAutophagy-Related ProteinsEndoplasmic ReticulumGene Expression Regulation, FungalMitochondriaMultiprotein ComplexesPhosphoprotein PhosphatasesPhosphorylationReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionAtg32 protein, S cerevisiaeAutophagy-Related ProteinsFAR11 protein, S cerevisiaeMultiprotein ComplexesPhosphoprotein PhosphatasesPPG1 protein, S cerevisiaeReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiae ProteinsAtg32autophagycell biologyFar complexmitophagyPpg1S. cerevisiaeSTRIPAK complex

Identifiers

PMID33317697
PMCPMC7738187
OpenAlexW3113274865

What OpenQuestion holds

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LicenceCC BY
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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 OpenQuestion graph.