Evidence map›Paper›PMID 34715013›Full record

ArticleMolecular cell2021

Structural basis of polyamine transport by human ATP13A2 (PARK9).

Sue Im Sim, Sören von Bülow, Gerhard Hummer, Eunyong Park

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.5field-weighted citation impact, top 9% 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

34 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. eIF5A and polyamines restrict mRNA levels in response to ribosome stalls.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Polyamine homeostasisbioRxiv : the preprint server for biology · 2025
    Article
  14. Article
  15. Article
  16. Review
  17. Metal Ion Signaling in Biomedicine.Chemical reviews · 2025
    Review
  18. Article
  19. The structure and function of P5A-ATPases.Nature communications · 2024
    Article
  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

4 authors at 4 institutions in 2 countries.

Sue Im SimDepartment of Molecular and Cell Biology, University of California Berkeley, Berkeley, CA 94720, USA.
Sören von BülowDepartment of Theoretical Biophysics, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany.
Gerhard HummerDepartment of Theoretical Biophysics, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany; Institute for Biophysics, Goethe University Frankfurt, 60438 Frankfurt am Main, Germany.
Eunyong ParkDepartment of Molecular and Cell Biology, University of California Berkeley, Berkeley, CA 94720, USA; California Institute for Quantitative Biosciences, University of California Berkeley, Berkeley, CA 94720, USA. Electronic address: eunyong_park@berkeley.edu.
Goethe University Frankfurt · DEMax Planck Institute of Biophysics · DEQB3 · USUniversity of California, Berkeley · US

Funding

MOLECULAR BIOPHYSICS TRAINING GRANTT32GM008295 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI HURLEY, JAMES H, WEMMER, DAVID E · 1989 to 2022
$8.1M
NIGMS NIH HHS T32 GM008295
6 · The paper itself

Abstract

Polyamines are small, organic polycations that are ubiquitous and essential to all forms of life. Currently, how polyamines are transported across membranes is not understood. Recent studies have suggested that ATP13A2 and its close homologs, collectively known as P5B-ATPases, are polyamine transporters at endo-/lysosomes. Loss-of-function mutations of ATP13A2 in humans cause hereditary early-onset Parkinson's disease. To understand the polyamine transport mechanism of ATP13A2, we determined high-resolution cryoelectron microscopy (cryo-EM) structures of human ATP13A2 in five distinct conformational intermediates, which together, represent a near-complete transport cycle of ATP13A2. The structural basis of the polyamine specificity was revealed by an endogenous polyamine molecule bound to a narrow, elongated cavity within the transmembrane domain. The structures show an atypical transport path for a water-soluble substrate, in which polyamines may exit within the cytosolic leaflet of the membrane. Our study provides important mechanistic insights into polyamine transport and a framework to understand the functions and mechanisms of P5B-ATPases.

Indexed as

AnimalsBiological TransportCatalysisCryoelectron MicroscopyCytosolHumansLipidsLysosomesMolecular Dynamics SimulationParkinson DiseasePhosphorylationPolyaminesProtein ConformationProtein DomainsProton-Translocating ATPasesSaccharomyces cerevisiaeATP13A2 protein, humanLipidsPolyaminesProton-Translocating ATPasescryo-EMlysosomemembrane proteinP5B-ATPaseParkinson's diseasepolyamineP-type ATPasesperminetransporter

Identifiers

PMID34715013
PMCPMC8604775
OpenAlexW3210296468

What OpenQuestion holds

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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.