Evidence map›Paper›PMID 35422486›Full record

ArticleNature communications2022

Proteolysis of adaptor protein Mmr1 during budding is necessary for mitochondrial homeostasis in Saccharomyces cerevisiae.

Keisuke Obara, Taku Yoshikawa, Ryu Yamaguchi, Keiko Kuwata, Kunio Nakatsukasa, Kohei Nishimura, Takumi Kamura

Abstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Keisuke Obara *Laboratory of Biological Science, Division of Natural Science, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8602, Japan. obara.keisuke.r2@f.mail.nagoya-u.ac.jp.
Taku Yoshikawa *Laboratory of Biological Science, Division of Natural Science, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8602, Japan.
Ryu YamaguchiLaboratory of Biological Science, Division of Natural Science, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8602, Japan.
Keiko KuwataInstitute of Transformative Bio-Molecules (ITbM), Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8601, Japan.
Kunio NakatsukasaGraduate School of Science, Nagoya City University, Yamanohata 1, Mizuho-cho, Mizuho-ku, Nagoya, 467-8501, Japan.ORCID 0000-0002-8894-051X
Kohei NishimuraLaboratory of Biological Science, Division of Natural Science, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8602, Japan.
Takumi KamuraLaboratory of Biological Science, Division of Natural Science, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, 464-8602, Japan. kamura.takumi.k1@f.mail.nagoya-u.ac.jp.ORCID 0000-0001-8541-447X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In yeast, mitochondria are passed on to daughter cells via the actin cable, motor protein Myo2, and adaptor protein Mmr1. They are released from the actin-myosin machinery after reaching the daughter cells. We report that Mmr1 is rapidly degraded by the ubiquitin-proteasome system in Saccharomyces cerevisiae. Redundant ubiquitin ligases Dma1 and Dma2 are responsible for Mmr1 ubiquitination. Dma1/2-mediated Mmr1 ubiquitination requires phosphorylation, most likely at S414 residue by Ste20 and Cla4. These kinases are mostly localized to the growing bud and nearly absent from mother cells, ensuring phosphorylation and ubiquitination of Mmr1 after the mitochondria enter the growing bud. In dma1Δ dma2Δ cells, transported mitochondria are first stacked at the bud-tip and then pulled back to the bud-neck. Stacked mitochondria in dma1Δ dma2Δ cells exhibit abnormal morphology, elevated respiratory activity, and increased level of reactive oxygen species, along with hypersensitivity to oxidative stresses. Collectively, spatiotemporally-regulated Mmr1 turnover guarantees mitochondrial homeostasis.

Indexed as

Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsActinsCell Cycle ProteinsHomeostasisMitochondriaMitochondrial ProteinsMyosinsProteolysisUbiquitinActinsCell Cycle ProteinsDma1 protein, S cerevisiaeDMA2 protein, S cerevisiaeMitochondrial ProteinsMmr1 protein, S cerevisiaeMyosinsSaccharomyces cerevisiae ProteinsUbiquitin

Identifiers

PMID35422486
PMCPMC9010424

What OpenQuestion holds

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Registered trials

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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.