Evidence map›Paper›PMID 23812165›Full record

ArticlePflugers Archiv : European journal of physiology2013

G protein modulation of K2P potassium channel TASK-2 : a role of basic residues in the C terminus domain.

Carolina Añazco, Gaspar Peña-Münzenmayer, Carla Araya, L Pablo Cid, Francisco V Sepúlveda, María Isabel Niemeyer

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In one paragraph

Article in Pflugers Archiv : European journal of physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Comparison of KHandbook of experimental pharmacology · 2021
    Article
  6. The Pharmacology of Two-Pore Domain Potassium Channels.Handbook of experimental pharmacology · 2021
    Article
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  9. KThe Journal of physiology · 2018
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  11. Review
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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

6 authors at 2 institutions in 2 countries.

Carolina AñazcoCentro de Estudios Científicos (CECs), Avenida Arturo Prat 514, Valdivia, Chile.
Gaspar Peña-Münzenmayer
Carla Araya
L Pablo Cid
Francisco V Sepúlveda
María Isabel Niemeyer
Centro de Estudios Científicos · CLNational Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TASK-2 (K2P5.1) is a background K(+) channel opened by extra- or intracellular alkalinisation that plays a role in renal bicarbonate handling, central chemoreception and cell volume regulation. Here, we present results that suggest that TASK-2 is also modulated by Gβγ subunits of heterotrimeric G protein. TASK-2 was strongly inhibited when GTP-γ-S was used as a replacement for intracellular GTP. No inhibition was present using GDP-β-S instead. Purified Gβγ introduced intracellularly also inhibited TASK-2 independently of whether GTP or GDP-β-S was present. The effects of GTP-γ-S and Gβγ subunits were abolished by neutralisation of TASK-2 C terminus double lysine residues K257-K258 or K296-K297. Use of membrane yeast two hybrid (MYTH) experiments and immunoprecipitation assays using tagged proteins gave evidence for a physical interaction between Gβ1 and Gβ2 subunits and TASK-2, in agreement with expression of these subunits in proximal tubule cells. Co-immunoprecipitation was impeded by mutating C terminus K257-K258 (but not K296-K297) to alanines. Gating by extra- or intracellular pH was unaltered in GTP-γ-S-insensitive TASK-2-K257A-K258A mutant. Shrinking TASK-2-expressing cells in hypertonic solution decreased the current to 36 % of its initial value. The same manoeuvre had a significantly diminished effect on TASK-2-K257A-K258A- or TASK-2-K296-K297-expressing cells, or in cells containing intracellular GDP-β-S. Our data are compatible with the concept that TASK-2 channels are modulated by Gβγ subunits of heterotrimeric G protein. We propose that this modulation is a novel way in which TASK-2 can be tuned to its physiological functions.

Indexed as

Amino Acid SequenceAnimalsGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsGuanosine DiphosphateHEK293 CellsHeterotrimeric GTP-Binding ProteinsHumansIon Channel GatingMicePotassium Channels, Tandem Pore DomainThionucleotidesTwo-Hybrid System TechniquesGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma Subunitsguanosine 5'-O-(2-thiodiphosphate)Guanosine DiphosphateHeterotrimeric GTP-Binding ProteinsKCNK1 protein, humanKcnk5 protein, mousePotassium Channels, Tandem Pore DomainThionucleotides

Identifiers

PMID23812165
OpenAlexW1240804144

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.