Evidence map›Paper›PMID 32973005›Full record

ArticleScience (New York, N.Y.)2020

The endoplasmic reticulum P5A-ATPase is a transmembrane helix dislocase.

Michael J McKenna, Sue Im Sim, Alban Ordureau, Lianjie Wei, J Wade Harper, Sichen Shao, Eunyong Park

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing 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

84 citing papers in PubMed.

  1. Article
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  5. Article
  6. Review
  7. The role of the nucleus in the control of mitochondrial precursor proteins in yeast.Protein science : a publication of the Protein Society · 2026
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Genetic Markers of Postmortem Brain Iron.Journal of neurochemistry · 2025
    Article
  17. Review
  18. Article
  19. Review
  20. The structure and function of P5A-ATPases.Nature communications · 2024
    Article

24 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

7 authors.

Michael J McKennaDepartment of Cell Biology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0002-8949-817X
Sue Im SimDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.ORCID 0000-0003-3560-101X
Alban OrdureauDepartment of Cell Biology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0002-4924-8520
Lianjie WeiDepartment of Cell Biology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USA.
J Wade HarperDepartment of Cell Biology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USA.ORCID 0000-0002-6944-7236
Sichen ShaoDepartment of Cell Biology, Blavatnik Institute, Harvard Medical School, Boston, MA 02115, USA. sichen_shao@hms.harvard.edu eunyong_park@berkeley.edu.ORCID 0000-0003-2679-5537
Eunyong ParkDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA. sichen_shao@hms.harvard.edu eunyong_park@berkeley.edu.ORCID 0000-0003-2994-5174

Funding

Endolysosomal Proteome Landscapes Through the Lens of Neurodegenerative Risk AllelesR01NS110395 · NINDS · HARVARD MEDICAL SCHOOL · PI JEFFREY W HARPER · 2018 to 2026
$4.1M
Systematic discovery and functional analysis of the PARKIN modified proteomeR37NS083524 · NINDS · HARVARD MEDICAL SCHOOL · PI HARPER, JEFFREY W · 2013 to 2019
$3.0M
Decoding ribosome-triggered quality control mechanismsDP2GM137415 · NIGMS · HARVARD MEDICAL SCHOOL · PI SHAO, SICHEN · 2019 to 2019
$2.5M
NIGMS NIH HHS DP2 GM137415NINDS NIH HHS R01 NS110395NINDS NIH HHS R37 NS083524
6 · The paper itself

Abstract

Organelle identity depends on protein composition. How mistargeted proteins are selectively recognized and removed from organelles is incompletely understood. Here, we found that the orphan P5A-adenosine triphosphatase (ATPase) transporter ATP13A1 (Spf1 in yeast) directly interacted with the transmembrane segment (TM) of mitochondrial tail-anchored proteins. P5A-ATPase activity mediated the extraction of mistargeted proteins from the endoplasmic reticulum (ER). Cryo-electron microscopy structures of

Indexed as

ATP-Binding Cassette TransportersCryoelectron MicroscopyEndoplasmic ReticulumHeLa CellsHumansMitochondrial MembranesProtein Conformation, alpha-HelicalProtein DomainsP-type ATPasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentATP13A1 protein, humanATP-Binding Cassette TransportersP-type ATPasesSaccharomyces cerevisiae ProteinsSPF1 protein, S cerevisiae

Identifiers

PMID32973005
PMCPMC8053355

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.