Evidence map›Paper›PMID 28920575›Full record

ArticleeLife2017

The P2X7 receptor forms a dye-permeable pore independent of its intracellular domain but dependent on membrane lipid composition.

Akira Karasawa, Kevin Michalski, Polina Mikhelzon, Toshimitsu Kawate

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
10.3field-weighted citation impact, top 1% 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

88 citing papers in PubMed, 144 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. P2XBritish journal of pharmacology · 2024
    Article
  13. Review
  14. P2X7 Variants in Pathophysiology.International journal of molecular sciences · 2024
    Review
  15. Review
  16. Article
  17. Two-pore potassium channel TREK-1 (K2P2.1) regulates NLRP3 inflammasome activity in macrophages.American journal of physiology. Lung cellular and molecular physiology · 2024
    Article
  18. Review
  19. Article
  20. Review

28 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

4 authors at 1 institution in 1 country.

Akira KarasawaDepartment of Molecular Medicine, Cornell University, Ithaca, United States.
Kevin MichalskiDepartment of Molecular Medicine, Cornell University, Ithaca, United States.
Polina MikhelzonDepartment of Molecular Medicine, Cornell University, Ithaca, United States.
Toshimitsu KawateDepartment of Molecular Medicine, Cornell University, Ithaca, United States.ORCID http://orcid.org/0000-0002-5005-2031
National Institutes of Health · US

Funding

TRAINING IN MOLECULAR PHYSICS OF BIOLOGICAL SYSTEMST32GM008267 · NIGMS · CORNELL UNIVERSITY ITHACA · PI WANG, MICHELLE D. · 1988 to 2021
$9.6M
Structure and Function of Pannexins: Activation MechanismR01GM114379 · NIGMS · CORNELL UNIVERSITY · PI KAWATE, TOSHIMITSU · 2015 to 2025
$3.1M
NIGMS NIH HHS R01 GM114379NIGMS NIH HHS T32 GM008267
6 · The paper itself

Abstract

The P2X7 receptor mediates extracellular ATP signaling implicated in the development of devastating diseases such as chronic pain and cancer. Activation of the P2X7 receptor leads to opening of the characteristic dye-permeable membrane pore for molecules up to ~900 Da. However, it remains controversial what constitutes this peculiar pore and how it opens. Here we show that the panda receptor, when purified and reconstituted into liposomes, forms an intrinsic dye-permeable pore in the absence of other cellular components. Unexpectedly, we found that this pore opens independent of its unique C-terminal domain. We also found that P2X7 channel activity is facilitated by phosphatidylglycerol and sphingomyelin, but dominantly inhibited by cholesterol through direct interactions with the transmembrane domain. In combination with cell-based functional studies, our data suggest that the P2X7 receptor itself constitutes a lipid-composition dependent dye-permeable pore, whose opening is facilitated by palmitoylated cysteines near the pore-lining helix.

Indexed as

AnimalsCell MembraneColoring AgentsMembrane LipidsPatch-Clamp TechniquesReceptors, Purinergic P2X7UrsidaeColoring AgentsMembrane LipidsReceptors, Purinergic P2X7biophysicscell linesdye uptakefunctional reconstitutiongiant pandaneurosciencenoneproteoliposomespurified ion channelstructural biology

Identifiers

PMID28920575
PMCPMC5624784
OpenAlexW2755544565

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.