Evidence map›Paper›PMID 38763336›Full record

ReviewThe Journal of biological chemistry2024

Consensus, controversies, and conundrums of P4-ATPases: The emerging face of eukaryotic lipid flippases.

H Diessel Duan, Huilin Li

Abstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Deciphering the language of mingling lipids and proteins.Current opinion in structural biology · 2025
    Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. The danger of flipping an outside lipid to the inside.Proceedings of the National Academy of Sciences of the United States of America · 2024
    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

2 authors.

H Diessel DuanDepartment of Structural Biology, Van Andel Institute, Grand Rapids, Michigan, USA. Electronic address: diessel.duan@vai.org.
Huilin LiDepartment of Structural Biology, Van Andel Institute, Grand Rapids, Michigan, USA. Electronic address: huilin.li@vai.org.

Funding

The structure and function of eukaryotic protein glycosylation enzymesR01CA231466 · NCI · VAN ANDEL RESEARCH INSTITUTE · PI Huilin Li · 2018 to 2026
$4.0M
NCI NIH HHS R01 CA231466
6 · The paper itself

Abstract

The cryo-EM resolution revolution has heralded a new era in our understanding of eukaryotic lipid flippases with a rapidly growing number of high-resolution structures. Flippases belong to the P4 family of ATPases (type IV P-type ATPases) that largely follow the reaction cycle proposed for the more extensively studied cation-transporting P-type ATPases. However, unlike the canonical P-type ATPases, no flippase cargos are transported in the phosphorylation half-reaction. Instead of being released into the intracellular or extracellular milieu, lipid cargos are transported to their destination at the inner leaflet of the membrane. Recent flippase structures have revealed multiple conformational states during the lipid transport cycle. Nonetheless, critical conformational states capturing the lipid cargo "in transit" are still missing. In this review, we highlight the amazing structural advances of these lipid transporters, discuss various perspectives on catalytic and regulatory mechanisms in the literature, and shed light on future directions in further deciphering the detailed molecular mechanisms of lipid flipping.

Indexed as

Adenosine TriphosphatasesAnimalsBiological TransportCryoelectron MicroscopyHumansLipid MetabolismPhospholipid Transfer ProteinsProtein ConformationAdenosine TriphosphatasesPhospholipid Transfer ProteinsATPaseautophosphorylationconformational changeflippaseinhibition mechanismlipid transportmembrane asymmetrymembrane curvaturemembrane traffickingP-type ATPase

Identifiers

PMID38763336
PMCPMC11225554

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Registered trials

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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.