Evidence map›Paper›PMID 23297214›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Voltage regulates adrenergic receptor function.

Andreas Rinne, Alexandra Birk, Moritz Bünemann

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

41 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Voltage Sensors Embedded in G Protein-Coupled Receptors.International journal of molecular sciences · 2024
    Review
  11. Anxiety and dysautonomia symptoms in patients with a NaClinical autonomic research : official journal of the Clinical Autonomic Research Society · 2024
    Article
  12. Review
  13. Article
  14. Article
  15. G Protein-Coupled Receptors Regulated by Membrane Potential.International journal of molecular sciences · 2022
    Review
  16. The activity of the serotonergic 5-HTThe Journal of biological chemistry · 2022
    Article
  17. Article
  18. Article
  19. Article
  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

3 authors at 1 institution in 1 country.

Andreas RinneInstitute of Pharmacology and Clinical Pharmacy, Biochemical Pharmacological Center Marburg, Philipps-University Marburg, 35043 Marburg, Germany.
Alexandra Birk
Moritz Bünemann
Philipps University of Marburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The present study demonstrates that agonist-mediated activation of α2A adrenergic receptors (α(2A)AR) is voltage-dependent. By resolving the kinetics of conformational changes of α(2A)AR at defined membrane potentials, we show that negative membrane potentials in the physiological range promote agonist-mediated activation of α(2A)AR. We discovered that the conformational change of α(2A)AR by voltage is independent from receptor-G protein docking and regulates receptor signaling, including β-arrestin binding, activation of G proteins, and G protein-activated inwardly rectifying K(+) currents. Comparison of the dynamics of voltage-dependence of clonidine- vs. norepinephrine-activated receptors uncovers interesting mechanistic insights. For norepinephrine, the time course of voltage-dependent deactivation reflected the deactivation kinetics of the receptor after agonist withdrawal and was strongly attenuated at saturating concentrations. In contrast, clonidine-activated α(2A)AR were switched by voltage even under fully saturating concentrations, and the kinetics of this switch was notably faster than dissociation of clonidine from α(2A)AR, indicating voltage-dependent regulation of the efficacy. We conclude that adrenergic receptors exhibit a unique, agonist-dependent mechanism of voltage-sensitivity that modulates downstream receptor signaling.

Indexed as

AnimalsArrestinsbeta-ArrestinsBiosensing TechniquesClonidineFluorescence Resonance Energy TransferG Protein-Coupled Inwardly-Rectifying Potassium ChannelsGTP-Binding ProteinsHEK293 CellsHumansKineticsMembrane PotentialsMiceNorepinephrineProtein ConformationRatsAdra2a protein, mouseArrestinsbeta-ArrestinsClonidineG Protein-Coupled Inwardly-Rectifying Potassium ChannelsGTP-Binding ProteinsNorepinephrineReceptors, Adrenergic, alpha-2Receptors, G-Protein-CoupledRecombinant Proteins

Identifiers

PMID23297214
PMCPMC3557066
OpenAlexW2035759650

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.