Evidence map›Paper›PMID 37980352›Full record

ArticleNature communications2023

Activation and substrate specificity of the human P4-ATPase ATP8B1.

Thibaud Dieudonné, Felix Kümmerer, Michelle Juknaviciute Laursen, Charlott Stock, Rasmus Kock Flygaard, Syma Khalid, Guillaume Lenoir, Joseph A Lyons, Kresten Lindorff-Larsen, Poul Nissen

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

24 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
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  12. ATP8B1 Deficiency Causes Phosphodiesterase 4-Mediated Glucagon Resistance and Impaired Gluconeogenesis in Mouse and Human Liver.Liver international : official journal of the International Association for the Study of the Liver · 2025
    Article
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  15. ATP8B1 regulates PIP2 localization and cleavage of pyroptotic executioner Gasdermin D.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. Deciphering the language of mingling lipids and proteins.Current opinion in structural biology · 2025
    Review
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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

10 authors at 4 institutions in 3 countries.

Thibaud DieudonnéDANDRITE, Nordic EMBL Partnership for Molecular Medicine, Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark. thibaud.dieudonne@i2bc.paris-saclay.fr.
Felix KümmererStructural Biology and NMR Laboratory & Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Copenhagen, Denmark.
Michelle Juknaviciute LaursenDANDRITE, Nordic EMBL Partnership for Molecular Medicine, Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.
Charlott StockDANDRITE, Nordic EMBL Partnership for Molecular Medicine, Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.ORCID 0000-0001-5471-3696
Rasmus Kock FlygaardDANDRITE, Nordic EMBL Partnership for Molecular Medicine, Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.
Syma KhalidDepartment of Biochemistry, University of Oxford, Oxford, UK.ORCID 0000-0002-3694-5044
Guillaume LenoirUniversité Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198, Gif-sur-Yvette, France.ORCID 0000-0002-8759-5179
Joseph A LyonsDepartment of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.ORCID 0000-0003-0218-4862
Kresten Lindorff-LarsenStructural Biology and NMR Laboratory & Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Copenhagen, Denmark.ORCID 0000-0002-4750-6039
Poul NissenDANDRITE, Nordic EMBL Partnership for Molecular Medicine, Department of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark. pn@mbg.au.dk.ORCID 0000-0003-0948-6628
Aarhus University · DKCentre National de la Recherche Scientifique · FRUniversity of Copenhagen · DKUniversity of Oxford · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Asymmetric distribution of phospholipids in eukaryotic membranes is essential for cell integrity, signaling pathways, and vesicular trafficking. P4-ATPases, also known as flippases, participate in creating and maintaining this asymmetry through active transport of phospholipids from the exoplasmic to the cytosolic leaflet. Here, we present a total of nine cryo-electron microscopy structures of the human flippase ATP8B1-CDC50A complex at 2.4 to 3.1 Å overall resolution, along with functional and computational studies, addressing the autophosphorylation steps from ATP, substrate recognition and occlusion, as well as a phosphoinositide binding site. We find that the P4-ATPase transport site is occupied by water upon phosphorylation from ATP. Additionally, we identify two different autoinhibited states, a closed and an outward-open conformation. Furthermore, we identify and characterize the PI(3,4,5)P

Indexed as

Adenosine TriphosphatasesPhospholipid Transfer ProteinsAdenosine TriphosphateCell MembraneCryoelectron MicroscopyHumansPhospholipidsSubstrate SpecificityAdenosine TriphosphatasesAdenosine TriphosphateATP8B1 protein, humanPhospholipidsPhospholipid Transfer Proteins

Identifiers

PMID37980352
PMCPMC10657443
OpenAlexW4388794978

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.