Evidence map›Paper›PMID 34172751›Full record

ArticleNature communications2021

Structure and transport mechanism of P5B-ATPases.

Ping Li, Kaituo Wang, Nina Salustros, Christina Grønberg, Pontus Gourdon

Abstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
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  5. Article
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  8. Article
  9. Review
  10. Article
  11. The structure and function of P5A-ATPases.Nature communications · 2024
    Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. ATP13A2 (PARK9) and basal ganglia function.Frontiers in neurology · 2023
    Review
  20. Article
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

5 authors.

Ping Li *Department of Experimental Medical Science, Lund University, Lund, Sweden.
Kaituo Wang *Department of Biomedical Sciences, University of Copenhagen, Copenhagen N, Denmark.ORCID 0000-0002-5922-7109
Nina SalustrosDepartment of Biomedical Sciences, University of Copenhagen, Copenhagen N, Denmark.
Christina GrønbergDepartment of Biomedical Sciences, University of Copenhagen, Copenhagen N, Denmark.
Pontus GourdonDepartment of Experimental Medical Science, Lund University, Lund, Sweden. pontus.gourdon@med.lu.se.ORCID 0000-0002-8631-3539

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In human cells, P5B-ATPases execute the active export of physiologically important polyamines such as spermine from lysosomes to the cytosol, a function linked to a palette of disorders. Yet, the overall shape of P5B-ATPases and the mechanisms of polyamine recognition, uptake and transport remain elusive. Here we describe a series of cryo-electron microscopy structures of a yeast homolog of human ATP13A2-5, Ypk9, determined at resolutions reaching 3.4 Å, and depicting three separate transport cycle intermediates, including spermine-bound conformations. Surprisingly, in the absence of cargo, Ypk9 rests in a phosphorylated conformation auto-inhibited by the N-terminus. Spermine uptake is accomplished through an electronegative cleft lined by transmembrane segments 2, 4 and 6. Despite the dramatically different nature of the transported cargo, these findings pinpoint shared principles of transport and regulation among the evolutionary related P4-, P5A- and P5B-ATPases. The data also provide a framework for analysis of associated maladies, such as Parkinson's disease.

Indexed as

Biological TransportChaetomiumCryoelectron MicroscopyFungal ProteinsModels, MolecularPhosphorylationProtein ConformationProton-Translocating ATPasesSpermineFungal ProteinsProton-Translocating ATPasesSpermine

Identifiers

PMID34172751
PMCPMC8233418

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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.