Evidence map›Paper›PMID 38818923›Full record

ArticleAutophagy2024

Atg44/Mdi1/mitofissin facilitates Dnm1-mediated mitochondrial fission.

Kentaro Furukawa, Manabu Hayatsu, Kentaro Okuyama, Tomoyuki Fukuda, Shun-Ichi Yamashita, Keiichi Inoue, Shinsuke Shibata, Tomotake Kanki

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 7 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed, 1 pooled it
–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

7 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Review
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  7. 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

8 authors.

Kentaro FurukawaDepartment of Cellular Physiology, Graduate School of Medical Sciences, Kyushu University, Fukuoka, Japan.ORCID 0000-0002-1551-1538
Manabu HayatsuDivision of Microscopic Anatomy, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.ORCID 0000-0002-5736-5612
Kentaro OkuyamaDivision of Microscopic Anatomy, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.ORCID 0000-0002-1231-7019
Tomoyuki FukudaDepartment of Cellular Physiology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.ORCID 0000-0003-2069-7127
Shun-Ichi YamashitaDepartment of Cellular Physiology, Graduate School of Medical Sciences, Kyushu University, Fukuoka, Japan.ORCID 0000-0001-8892-0765
Keiichi InoueDepartment of Cellular Physiology, Graduate School of Medical Sciences, Kyushu University, Fukuoka, Japan.ORCID 0000-0002-7101-486X
Shinsuke ShibataDivision of Microscopic Anatomy, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.ORCID 0000-0002-1185-9043
Tomotake KankiDepartment of Cellular Physiology, Graduate School of Medical Sciences, Kyushu University, Fukuoka, Japan.ORCID 0000-0001-9646-5379

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondria undergo fission and fusion, and their coordinated balance is crucial for maintaining mitochondrial homeostasis. In yeast, the dynamin-related protein Dnm1 is a mitochondrial fission factor acting from outside the mitochondria. We recently reported the mitochondrial intermembrane space protein Atg44/mitofissin/Mdi1/Mco8 as a novel fission factor, but the relationship between Atg44 and Dnm1 remains elusive. Here, we show that Atg44 is required to complete Dnm1-mediated mitochondrial fission under homeostatic conditions. Atg44-deficient cells often exhibit enlarged mitochondria with accumulated Dnm1 and rosary-like mitochondria with Dnm1 foci at constriction sites. These mitochondrial constriction sites retain the continuity of both the outer and inner membranes within an extremely confined space, indicating that Dnm1 is unable to complete mitochondrial fission without Atg44. Moreover, accumulated Atg44 proteins are observed at mitochondrial constriction sites. These findings suggest that Atg44 and Dnm1 cooperatively execute mitochondrial fission from inside and outside the mitochondria, respectively.

Indexed as

MitochondriaMitochondrial DynamicsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAutophagyAutophagy-Related ProteinsDynaminsEndoplasmic ReticulumGTP PhosphohydrolasesMitochondrial ProteinsAutophagy-Related ProteinsDNM1 protein, S cerevisiaeDynaminsGTP PhosphohydrolasesMitochondrial ProteinsSaccharomyces cerevisiae ProteinsAtg44Dnm1mitochondrial fissionmitofissinmitophagyyeast

Identifiers

PMID38818923
PMCPMC11423663

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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.