Evidence map›Paper›PMID 30237312›Full record

ArticleThe EMBO journal2018

Syntaxin 17 regulates the localization and function of PGAM5 in mitochondrial division and mitophagy.

Masashi Sugo, Hana Kimura, Kohei Arasaki, Toshiki Amemiya, Naohiko Hirota, Naoshi Dohmae, Yuzuru Imai, Tsuyoshi Inoshita, Kahori Shiba-Fukushima, Nobutaka Hattori and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed, 1 pooled it
3.6field-weighted citation impact, top 6% 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

62 citing papers in PubMed, 1 synthesis or guideline pooled it, 107 citations in OpenAlex.

  1. Guideline
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Autophagy-Mediated Suppression of Tumor Growth by Food-Grade Lipid Nanoparticles in Mice.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Histidine Phosphorylation: Protein Kinases and Phosphatases.International journal of molecular sciences · 2024
    Review
  19. Mitophagy and spermatogenesis: Role and mechanisms.Biochemistry and biophysics reports · 2024
    Review
  20. Article

2 more citing papers are in PubMed but not listed here.

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

15 authors at 4 institutions in 1 country.

Masashi SugoSchool of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, Japan.
Hana KimuraSchool of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, Japan.
Kohei ArasakiSchool of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, Japan karasaki@toyaku.ac.jp tagaya@toyaku.ac.jp.ORCID 0000-0003-0647-3565
Toshiki AmemiyaSchool of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, Japan.
Naohiko HirotaSchool of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, Japan.
Naoshi DohmaeBiomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, Japan.
Yuzuru ImaiDepartment of Research for Parkinson's Disease, Juntendo University Graduate School of Medicine, Tokyo, Japan.
Tsuyoshi InoshitaDepartment of Treatment and Research in Multiple Sclerosis and Neuro-intractable Disease, Juntendo University Graduate School of Medicine, Tokyo, Japan.
Kahori Shiba-FukushimaDepartment of Treatment and Research in Multiple Sclerosis and Neuro-intractable Disease, Juntendo University Graduate School of Medicine, Tokyo, Japan.
Nobutaka HattoriDepartment of Research for Parkinson's Disease, Juntendo University Graduate School of Medicine, Tokyo, Japan.
Jinglei ChengDepartment of Anatomy and Molecular Cell Biology, Nagoya University Graduate School of Medicine, Nagoya, Japan.
Toyoshi FujimotoDepartment of Anatomy and Molecular Cell Biology, Nagoya University Graduate School of Medicine, Nagoya, Japan.
Yuichi WakanaSchool of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, Japan.
Hiroki InoueSchool of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, Japan.
Mitsuo TagayaSchool of Life Sciences, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, Japan karasaki@toyaku.ac.jp tagaya@toyaku.ac.jp.ORCID 0000-0001-9137-7142
Tokyo University of Pharmacy and Life Sciences · JPJuntendo University · JPNagoya University · JPRIKEN Center for Sustainable Resource Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PGAM5, a mitochondrial protein phosphatase that is genetically and biochemically linked to PINK1, facilitates mitochondrial division by dephosphorylating the mitochondrial fission factor Drp1. At the onset of mitophagy, PGAM5 is cleaved by PARL, a rhomboid protease that degrades PINK1 in healthy cells, and the cleaved form facilitates the engulfment of damaged mitochondria by autophagosomes by dephosphorylating the mitophagy receptor FUNDC1. Here, we show that the function and localization of PGAM5 are regulated by syntaxin 17 (Stx17), a mitochondria-associated membrane/mitochondria protein implicated in mitochondrial dynamics in fed cells and autophagy in starved cells. In healthy cells, loss of Stx17 causes PGAM5 aggregation within mitochondria and thereby failure of the dephosphorylation of Drp1, leading to mitochondrial elongation. In Parkin-mediated mitophagy, Stx17 is prerequisite for PGAM5 to interact with FUNDC1. Our results reveal that the Stx17-PGAM5 axis plays pivotal roles in mitochondrial division and PINK1/Parkin-mediated mitophagy.

Indexed as

Mitochondrial DynamicsMitophagySignal TransductionAutophagosomesDynaminsGTP PhosphohydrolasesHeLa CellsHumansMembrane ProteinsMetalloproteasesMicrotubule-Associated ProteinsMitochondrial ProteinsPhosphoprotein PhosphatasesProtein KinasesProteolysisPTEN-Induced Putative KinaseDNM1L protein, humanDynaminsFUNDC1 protein, humanGTP PhosphohydrolasesMembrane ProteinsMetalloproteasesMicrotubule-Associated ProteinsMitochondrial Proteinsparkin proteinPARL protein, humanPGAM5 protein, humanPhosphoprotein PhosphatasesProtein KinasesPTEN-Induced Putative KinaseQa-SNARE ProteinsSTX17 protein, humanUbiquitin-Protein Ligasesautophagy receptormitochondria‐associated membranemitochondrial divisionmitophagyprotein phosphatase

Identifiers

PMID30237312
PMCPMC6213275
OpenAlexW2890597757

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.