Evidence map›Paper›PMID 24904274›Full record

ReviewFrontiers in molecular neuroscience2014

Cellular function and pathological role of ATP13A2 and related P-type transport ATPases in Parkinson's disease and other neurological disorders.

Sarah van Veen, Danny M Sørensen, Tine Holemans, Henrik W Holen, Michael G Palmgren, Peter Vangheluwe

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in molecular neuroscience, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed, 1 pooled it
7.2field-weighted citation impact, top 2% 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

55 citing papers in PubMed, 1 synthesis or guideline pooled it, 86 citations in OpenAlex.

  1. Pooled it
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  19. The Non-Gastric HInternational journal of molecular sciences · 2022
    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

6 authors at 2 institutions in 2 countries.

Sarah van VeenLaboratory of Cellular Transport Systems, Department of Cellular and Molecular Medicine, KU Leuven Leuven, Belgium.
Danny M SørensenLaboratory of Cellular Transport Systems, Department of Cellular and Molecular Medicine, KU Leuven Leuven, Belgium.
Tine HolemansLaboratory of Cellular Transport Systems, Department of Cellular and Molecular Medicine, KU Leuven Leuven, Belgium.
Henrik W HolenDepartment of Plant and Environmental Sciences, Centre for Membrane Pumps in Cells and Disease - PUMPkin, University of Copenhagen Frederiksberg, Denmark.
Michael G PalmgrenDepartment of Plant and Environmental Sciences, Centre for Membrane Pumps in Cells and Disease - PUMPkin, University of Copenhagen Frederiksberg, Denmark.
Peter VangheluweLaboratory of Cellular Transport Systems, Department of Cellular and Molecular Medicine, KU Leuven Leuven, Belgium.
KU Leuven · BEUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mutations in ATP13A2 lead to Kufor-Rakeb syndrome, a parkinsonism with dementia. ATP13A2 belongs to the P-type transport ATPases, a large family of primary active transporters that exert vital cellular functions. However, the cellular function and transported substrate of ATP13A2 remain unknown. To discuss the role of ATP13A2 in neurodegeneration, we first provide a short description of the architecture and transport mechanism of P-type transport ATPases. Then, we briefly highlight key P-type ATPases involved in neuronal disorders such as the copper transporters ATP7A (Menkes disease), ATP7B (Wilson disease), the Na(+)/K(+)-ATPases ATP1A2 (familial hemiplegic migraine) and ATP1A3 (rapid-onset dystonia parkinsonism). Finally, we review the recent literature of ATP13A2 and discuss ATP13A2's putative cellular function in the light of what is known concerning the functions of other, better-studied P-type ATPases. We critically review the available data concerning the role of ATP13A2 in heavy metal transport and propose a possible alternative hypothesis that ATP13A2 might be a flippase. As a flippase, ATP13A2 may transport an organic molecule, such as a lipid or a peptide, from one membrane leaflet to the other. A flippase might control local lipid dynamics during vesicle formation and membrane fusion events.

Indexed as

alpha-synucleindystoniaflippaseheavy metal toxicitylysosomemitochondriamitophagyparkinsonism

Identifiers

PMID24904274
PMCPMC4033846
OpenAlexW2036697195

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.