Evidence map›Paper›PMID 26567335›Full record

ArticleThe Journal of biological chemistry2016

Human Type IV P-type ATPases That Work as Plasma Membrane Phospholipid Flippases and Their Regulation by Caspase and Calcium.

Katsumori Segawa, Sachiko Kurata, Shigekazu Nagata

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

90 citing papers in PubMed, 138 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Metabolic Control of Membrane Lipid Asymmetry in Cancer.International journal of molecular sciences · 2026
    Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Loss of lipid asymmetry facilitates plasma membrane blebbing by decreasing membrane lipid packing.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Lipid probes to study ion channels.Current opinion in chemical biology · 2025
    Review
  12. Review
  13. The Surface Proteome of Bovine Unsexed and Sexed Spermatozoa.Animals : an open access journal from MDPI · 2025
    Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

30 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Katsumori SegawaFrom the Laboratory of Biochemistry & Immunology, Immunology Frontier Research Center, Osaka University, Suita, Osaka 565-0871, Japan.
Sachiko KurataFrom the Laboratory of Biochemistry & Immunology, Immunology Frontier Research Center, Osaka University, Suita, Osaka 565-0871, Japan.
Shigekazu NagataFrom the Laboratory of Biochemistry & Immunology, Immunology Frontier Research Center, Osaka University, Suita, Osaka 565-0871, Japan snagata@ifrec.osaka-u.ac.jp.
Osaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In plasma membranes, flippases translocate aminophospholipids such as phosphatidylserine and phosphatidylethanolamine from the extracellular to the cytoplasmic leaflet. Mammalian ATP11C, a type IV P-type ATPase, acts as a flippase at the plasma membrane. Here, by expressing 12 human type IV P-type ATPases in ATP11C-deficient cells, we determined that ATP8A2 and ATP11A can also act as plasma membrane flippases. As with ATP11C, ATP8A2 and ATP11A localized to the plasma membrane in a CDC50A-dependent manner. ATP11A was cleaved by caspases during apoptosis, and a caspase-resistant ATP11A blocked apoptotic PtdSer exposure. In contrast, ATP8A2 was not cleaved by caspase, and cells expressing ATP8A2 did not expose PtdSer during apoptosis. Similarly, high Ca(2+) concentrations inhibited the ATP11A and ATP11C PtdSer flippase activity, but ATP8A2 flippase activity was relatively resistant to Ca(2+). ATP11A and ATP11C were ubiquitously expressed in human and mouse adult tissues. In contrast, ATP8A2 was expressed in specific tissues, such as the brain and testis. Thus, ATP8A2 may play a specific role in translocating PtdSer in these tissues.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceAnimalsApoptosisCalciumCaspase 3Cell LineCell MembraneHumansMice, Inbred C57BLMolecular Sequence DataPhosphatidylserinesPhospholipid Transfer ProteinsSubcellular FractionsTissue DistributionAdenosine TriphosphatasesCalciumCaspase 3PhosphatidylserinesPhospholipid Transfer ProteinsapoptosiscalciumcaspaseflippaseP4-ATPasephosphatidylserineplasma membrane

Identifiers

PMID26567335
PMCPMC4705396
OpenAlexW2224482007

What OpenQuestion holds

Textmetadata
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.