Evidence map›Paper›PMID 40841558›Full record

ArticleNature communications2025

Control of Golgi- V-ATPase through Sac1-dependent co-regulation of PI(4)P and cholesterol.

Xin Zhou, Miesje M van der Stoel, Shreyas Kaptan, Haoran Li, Shiqian Li, Maarit Hölttä, Helena Vihinen, Eija Jokitalo, Christoph Thiele, Olli Pietiläinen and 5 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. 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

15 authors.

Xin Zhou *Stem Cells and Metabolism Research Program and Department of Anatomy, Faculty of Medicine, University of Helsinki, Helsinki, Finland.ORCID http://orcid.org/0000-0002-6942-4800
Miesje M van der Stoel *Stem Cells and Metabolism Research Program and Department of Anatomy, Faculty of Medicine, University of Helsinki, Helsinki, Finland.ORCID http://orcid.org/0000-0003-4245-2497
Shreyas KaptanDepartment of Physics, University of Helsinki, Helsinki, Finland.
Haoran LiStem Cells and Metabolism Research Program and Department of Anatomy, Faculty of Medicine, University of Helsinki, Helsinki, Finland.
Shiqian LiStem Cells and Metabolism Research Program and Department of Anatomy, Faculty of Medicine, University of Helsinki, Helsinki, Finland.
Maarit HölttäStem Cells and Metabolism Research Program and Department of Anatomy, Faculty of Medicine, University of Helsinki, Helsinki, Finland.ORCID http://orcid.org/0000-0002-0488-4486
Helena VihinenInstitute of Biotechnology, University of Helsinki, Helsinki, Finland.ORCID http://orcid.org/0000-0003-3862-9237
Eija JokitaloInstitute of Biotechnology, University of Helsinki, Helsinki, Finland.ORCID http://orcid.org/0000-0002-4159-6934
Christoph ThieleLife and Medical Science Institute, University of Bonn, Bonn, Germany.ORCID http://orcid.org/0000-0001-5161-2558
Olli PietiläinenNeuroscience Center, Helsinki Institute of Life Science, University of Helsinki, Helsinki, Finland.ORCID http://orcid.org/0000-0003-4387-1861
Shin MoriokaMedical Research Institute, Tokyo Medical and Dental University, Tokyo, Japan.ORCID http://orcid.org/0000-0002-7702-0937
Junko SasakiMedical Research Institute, Tokyo Medical and Dental University, Tokyo, Japan.
Takehiko SasakiMedical Research Institute, Tokyo Medical and Dental University, Tokyo, Japan.ORCID http://orcid.org/0000-0003-1837-3748
Ilpo VattulainenDepartment of Physics, University of Helsinki, Helsinki, Finland.ORCID http://orcid.org/0000-0001-7408-3214
Elina IkonenStem Cells and Metabolism Research Program and Department of Anatomy, Faculty of Medicine, University of Helsinki, Helsinki, Finland. elina.ikonen@helsinki.fi.ORCID http://orcid.org/0000-0001-8382-1135

Funding

Academy of Finland (Suomen Akatemia) 364185Wellcome Trust 332096
6 · The paper itself

Abstract

Sac1 is a conserved phosphoinositide phosphatase, whose loss-of-function compromises cell and organism viability. Here, we employ acute auxin-inducible Sac1 degradation to identify its immediate downstream effectors in human cells. Most of Sac1 is degraded in ~1 h, paralleled by increased PI(4)P and decreased cholesterol in the trans-Golgi network (TGN) during the following hour, and superseded by Golgi fragmentation, impaired glycosylation, and selective degradation of TGN proteins by ~4 h. The TGN disintegration results from its acute deacidification caused by disassembly of the Golgi V-ATPase. Mechanistically, Sac1 mediated TGN membrane composition maintains an assembly-promoting conformation of the V

Indexed as

CholesterolGolgi ApparatusPhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesVacuolar Proton-Translocating ATPasesGlycosylationHEK293 CellsHeLa CellsHumansIndoleacetic AcidsMembrane Proteinstrans-Golgi NetworkTrophoblastsCholesterolIndoleacetic AcidsMembrane Proteinsphosphatidylinositol 4-phosphatePhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesSac1 protein, mammalianVacuolar Proton-Translocating ATPases

Identifiers

PMID40841558
PMCPMC12371084

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.