Evidence map›Paper›PMID 35349344›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Structural insights into the activation of autoinhibited human lipid flippase ATP8B1 upon substrate binding.

Meng-Ting Cheng, Yu Chen, Zhi-Peng Chen, Xin Liu, Zhiyong Zhang, Yuxing Chen, Wen-Tao Hou, Cong-Zhao Zhou

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.8field-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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. 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
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Molecular and cellular biology · 2024
    Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Functional Analysis of the P-Type ATPases Apt2-4 fromJournal of fungi (Basel, Switzerland) · 2023
    Article
  19. Review
  20. Review
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

8 authors at 1 institution in 1 country.

Meng-Ting ChengSchool of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230027, China.ORCID 0000-0003-4616-7124
Yu ChenSchool of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230027, China.ORCID 0000-0001-9206-7808
Zhi-Peng ChenSchool of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230027, China.
Xin LiuSchool of Data Science, University of Science and Technology of China, Hefei 230026, China.ORCID 0000-0001-9728-0093
Zhiyong ZhangSchool of Data Science, University of Science and Technology of China, Hefei 230026, China.ORCID 0000-0001-8202-9672
Yuxing ChenSchool of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230027, China.ORCID 0000-0002-7560-1922
Wen-Tao HouSchool of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230027, China.
Cong-Zhao ZhouSchool of Life Sciences, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei 230027, China.
University of Science and Technology of China · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SignificanceATP8B1 is a P4 ATPase that maintains membrane asymmetry by transporting phospholipids across the cell membrane. Disturbance of lipid asymmetry will lead to the imbalance of the cell membrane and eventually, cell death. Thus, defects in ATP8B1 are usually associated with severe human diseases, such as intrahepatic cholestasis. The present structures of ATP8B1 complexed with its auxiliary noncatalytic partners CDC50A and CDC50B reveal an autoinhibited state of ATP8B1 that could be released upon substrate binding. Moreover, release of this autoinhibition could be facilitated by the bile acids, which are key factors that alter the membrane asymmetry of hepatocytes. This enabled us to figure out a feedback loop of bile acids and lipids across the cell membrane.

Indexed as

Adenosine TriphosphatasesCholestasis, IntrahepaticBile Acids and SaltsCell MembraneHumansPhospholipidsPhospholipid Transfer ProteinsAdenosine TriphosphatasesATP8B1 protein, humanBile Acids and SaltsPhospholipidsPhospholipid Transfer ProteinsATP8B1bile acidcryo-EM structureP4 ATPasephospholipid flippase

Identifiers

PMID35349344
PMCPMC9168909
OpenAlexW4225650797

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.