Evidence map›Paper›PMID 21757694›Full record

ArticleThe Journal of biological chemistry2011

Identification of human P2X1 receptor-interacting proteins reveals a role of the cytoskeleton in receptor regulation.

Ulyana Lalo, Jonathan A Roberts, Richard J Evans

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. 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
2.8field-weighted citation impact, top 11% 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

13 citing papers in PubMed, 25 citations in OpenAlex.

  1. Trial
  2. Article
  3. Regulation of P2X1 receptors by modulators of the cAMP effectors PKA and EPAC.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  4. Article
  5. CaThe Journal of biological chemistry · 2019
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. The trafficking and targeting of P2X receptors.Frontiers in cellular neuroscience · 2013
    Review
  11. Article
  12. Review
  13. 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

3 authors at 1 institution in 1 country.

Ulyana LaloDepartment of Cell Physiology and Pharmacology, Henry Wellcome Building, University of Leicester, Leicester LE1 9HN, United Kingdom.
Jonathan A RobertsDepartment of Cell Physiology and Pharmacology, Henry Wellcome Building, University of Leicester, Leicester LE1 9HN, United Kingdom.
Richard J EvansDepartment of Cell Physiology and Pharmacology, Henry Wellcome Building, University of Leicester, Leicester LE1 9HN, United Kingdom. Electronic address: rje6@le.ac.uk.
University of Leicester · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

P2X1 receptors are ATP-gated ion channels expressed by smooth muscle and blood cells. Carboxyl-terminally His-FLAG-tagged human P2X1 receptors were stably expressed in HEK293 cells and co-purified with cytoskeletal proteins including actin. Disruption of the actin cytoskeleton with cytochalasin D inhibited P2X1 receptor currents with no effect on the time course of the response or surface expression of the receptor. Stabilization of the cytoskeleton with jasplakinolide had no effect on P2X1 receptor currents but decreased receptor mobility. P2X2 receptor currents were unaffected by cytochalasin, and P2X1/2 receptor chimeras were used to identify the molecular basis of actin sensitivity. These studies showed that the intracellular amino terminus accounts for the inhibitory effects of cytoskeletal disruption similar to that shown for lipid raft/cholesterol sensitivity. Stabilization of the cytoskeleton with jasplakinolide abolished the inhibitory effects of cholesterol depletion on P2X1 receptor currents, suggesting that lipid rafts may regulate the receptor through stabilization of the cytoskeleton. These studies show that the cytoskeleton plays an important role in P2X1 receptor regulation.

Indexed as

Gene Expression RegulationActinsAdenosine TriphosphateAnimalsCytochalasin DCytoskeletonDepsipeptidesElectrophysiologyHEK293 CellsHumansMembrane MicrodomainsMicroscopy, ConfocalModels, BiologicalMyocytes, Smooth MuscleProtein Kinase CProtein Structure, TertiaryActinsAdenosine TriphosphateCytochalasin DDepsipeptidesjasplakinolideProtein Kinase CReceptors, Purinergic P2X1

Identifiers

PMID21757694
PMCPMC3162419
OpenAlexW2088916399

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.