Evidence map›Paper›PMID 37072500›Full record

ArticleCommunications biology2023

Spatial and temporal dynamics of ATP synthase from mitochondria toward the cell surface.

Yi-Wen Chang, T Tony Yang, Min-Chun Chen, Y-Geh Liaw, Chieh-Fan Yin, Xiu-Qi Lin-Yan, Ting-Yu Huang, Jen-Tzu Hou, Yi-Hsuan Hung, Chia-Lang Hsu and 2 more

Abstract read
In one paragraph

Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
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  7. Review
  8. Article
  9. Aspirin Combined with Antifungal Drugs SuppressesJournal of microbiology and biotechnology · 2025
    Article
  10. Review
  11. Review
  12. Article
  13. Article
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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

12 authors.

Yi-Wen ChangDepartment of Life Science, Institute of Molecular and Cellular Biology, National Taiwan University, Taipei, 106, Taiwan.ORCID 0000-0003-3215-1674
T Tony YangDepartment of Electrical Engineering, National Taiwan University, Taipei, 106, Taiwan.ORCID 0000-0002-6462-394X
Min-Chun ChenDepartment of Life Science, Institute of Molecular and Cellular Biology, National Taiwan University, Taipei, 106, Taiwan.
Y-Geh LiawDepartment of Life Science, Institute of Molecular and Cellular Biology, National Taiwan University, Taipei, 106, Taiwan.
Chieh-Fan YinDepartment of Life Science, Institute of Molecular and Cellular Biology, National Taiwan University, Taipei, 106, Taiwan.
Xiu-Qi Lin-YanDepartment of Life Science, Institute of Molecular and Cellular Biology, National Taiwan University, Taipei, 106, Taiwan.
Ting-Yu HuangDepartment of Life Science, Institute of Molecular and Cellular Biology, National Taiwan University, Taipei, 106, Taiwan.
Jen-Tzu HouDepartment of Life Science, Institute of Molecular and Cellular Biology, National Taiwan University, Taipei, 106, Taiwan.
Yi-Hsuan HungDepartment of Life Science, Institute of Molecular and Cellular Biology, National Taiwan University, Taipei, 106, Taiwan.
Chia-Lang HsuDepartment of Life Science, Institute of Molecular and Cellular Biology, National Taiwan University, Taipei, 106, Taiwan.ORCID 0000-0002-7447-8045
Hsuan-Cheng HuangInstitute of Biomedical Informatics, National Yang Ming Chiao Tung University, Taipei, 112, Taiwan. hsuancheng@nycu.edu.tw.ORCID 0000-0002-3386-0934
Hsueh-Fen JuanDepartment of Life Science, Institute of Molecular and Cellular Biology, National Taiwan University, Taipei, 106, Taiwan. yukijuan@ntu.edu.tw.ORCID 0000-0003-4876-3309

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ectopic ATP synthase complex (eATP synthase), located on cancer cell surface, has been reported to possess catalytic activity that facilitates the generation of ATP in the extracellular environment to establish a suitable microenvironment and to be a potential target for cancer therapy. However, the mechanism of intracellular ATP synthase complex transport remains unclear. Using a combination of spatial proteomics, interaction proteomics, and transcriptomics analyses, we find ATP synthase complex is first assembled in the mitochondria and subsequently delivered to the cell surface along the microtubule via the interplay of dynamin-related protein 1 (DRP1) and kinesin family member 5B (KIF5B). We further demonstrate that the mitochondrial membrane fuses to the plasma membrane in turn to anchor ATP syntheses on the cell surface using super-resolution imaging and real-time fusion assay in live cells. Our results provide a blueprint of eATP synthase trafficking and contribute to the understanding of the dynamics of tumor progression.

Indexed as

MitochondriaNeoplasmsAdenosine TriphosphateCell MembraneHumansMitochondrial MembranesTumor MicroenvironmentAdenosine Triphosphate

Identifiers

PMID37072500
PMCPMC10113393

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.