Evidence map›Paper›PMID 33276429›Full record

ArticleInternational journal of molecular sciences2020

Stretch-Induced Activation of Pannexin 1 Channels Can Be Prevented by PKA-Dependent Phosphorylation.

Ximena López, Rosalba Escamilla, Paola Fernández, Yorley Duarte, Fernando González-Nilo, Nicolás Palacios-Prado, Agustín D Martinez, Juan C Sáez

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

24 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Article
  3. Pannexins in the vasculature.American journal of physiology. Heart and circulatory physiology · 2025
    Review
  4. Pannexin channels in the kidney.American journal of physiology. Renal physiology · 2025
    Review
  5. Article
  6. Pannexin channels in inflammation and tumorigenesis.Frontiers in cell and developmental biology · 2025
    Review
  7. Review
  8. CaProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Unnexin is a protein subunit of a large-pore channel expressed by unicellular organisms.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Article
  18. Pannexin1 channels in the liver: an open enemy.Frontiers in cell and developmental biology · 2023
    Review
  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 3 institutions in 1 country.

Ximena LópezDepartamento de Fisiología, Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, Santiago 8331150, Chile.
Rosalba EscamillaFacultad de Ciencias, Instituto de Neurociencias and Centro Interdisciplinario de Neurociencias de Valparaíso, Universidad de Valparaíso, Valparaíso 2381850, Chile.ORCID 0000-0002-4491-3907
Paola FernándezFacultad de Ciencias, Instituto de Neurociencias and Centro Interdisciplinario de Neurociencias de Valparaíso, Universidad de Valparaíso, Valparaíso 2381850, Chile.
Yorley DuarteFacultad de Ciencias, Instituto de Neurociencias and Centro Interdisciplinario de Neurociencias de Valparaíso, Universidad de Valparaíso, Valparaíso 2381850, Chile.
Fernando González-NiloFacultad de Ciencias, Instituto de Neurociencias and Centro Interdisciplinario de Neurociencias de Valparaíso, Universidad de Valparaíso, Valparaíso 2381850, Chile.ORCID 0000-0001-6857-3575
Nicolás Palacios-PradoDepartamento de Fisiología, Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, Santiago 8331150, Chile.ORCID 0000-0002-3411-8002
Agustín D MartinezFacultad de Ciencias, Instituto de Neurociencias and Centro Interdisciplinario de Neurociencias de Valparaíso, Universidad de Valparaíso, Valparaíso 2381850, Chile.
Juan C SáezDepartamento de Fisiología, Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, Santiago 8331150, Chile.
Pontificia Universidad Católica de Chile · CLUniversity of Valparaíso · CLUniversidad Andrés Bello · CL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pannexin 1 channels located in the cell membrane are permeable to ions, metabolites, and signaling molecules. While the activity of these channels is known to be modulated by phosphorylation on T198, T308, and S206, the possible involvement of other putative phosphorylation sites remains unknown. Here, we describe that the activity of Panx1 channels induced by mechanical stretch is reduced by adenosine via a PKA-dependent pathway. The mechanical stretch-induced activity-measured by changes in DAPI uptake-of Panx1 channels expressed in HeLa cell transfectants was inhibited by adenosine or cAMP analogs that permeate the cell membrane. Moreover, inhibition of PKA but not PKC, p38 MAPK, Akt, or PKG prevented the effects of cAMP analogs, suggesting the involvement of Panx1 phosphorylation by PKA. Accordingly, alanine substitution of T302 or S328, two putative PKA phosphorylation sites, prevented the inhibitory effect of cAMP analogs. Moreover, phosphomimetic mutation of either T302 or S328 to aspartate prevented the mechanical stretch-induced activation of Panx1 channels. A molecular dynamics simulation revealed that T302 and S328 are located in the water-lipid interphase near the lateral tunnel of the intracellular region, suggesting that their phosphorylation could promote conformational changes in lateral tunnels. Thus, Panx1 phosphorylation via PKA could be modulated by G protein-coupled receptors associated with the Gs subunit.

Indexed as

Ion Channel GatingMechanotransduction, CellularConnexinsCyclic AMP-Dependent Protein KinasesHeLa CellsHumansModels, MolecularMutagenesis, Site-DirectedNerve Tissue ProteinsPhosphorylationProtein ConformationStructure-Activity RelationshipConnexinsCyclic AMP-Dependent Protein KinasesNerve Tissue ProteinsPANX1 protein, humanadenosinecAMPdye uptakeprotein phosphorylationsite-directed mutation

Identifiers

PMID33276429
PMCPMC7731223
OpenAlexW3109596145

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.