Evidence map›Paper›PMID 26013830›Full record

ArticleThe Journal of biological chemistry2015

Human CLC-K Channels Require Palmitoylation of Their Accessory Subunit Barttin to Be Functional.

Kim Vanessa Steinke, Nataliya Gorinski, Daniel Wojciechowski, Vladimir Todorov, Daria Guseva, Evgeni Ponimaskin, Christoph Fahlke, Martin Fischer

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Biomolecules · 2023
    Review
  5. Palmitoylation of Voltage-Gated Ion Channels.International journal of molecular sciences · 2022
    Review
  6. Article
  7. Article
  8. Article
  9. New Insights into the Mechanism of NOJournal of the American Society of Nephrology : JASN · 2019
    Article
  10. Article
  11. Article
  12. Article
  13. New perspective of ClC-Kb/2 Cl- channel physiology in the distal renal tubule.American journal of physiology. Renal physiology · 2016
    Review
  14. Review
  15. 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

8 authors at 3 institutions in 1 country.

Kim Vanessa SteinkeFrom the Institut für Neurophysiologie, Medizinische Hochschule Hannover, 30625 Hannover, Germany.
Nataliya GorinskiFrom the Institut für Neurophysiologie, Medizinische Hochschule Hannover, 30625 Hannover, Germany.
Daniel WojciechowskiFrom the Institut für Neurophysiologie, Medizinische Hochschule Hannover, 30625 Hannover, Germany, Institute of Complex Systems, Zelluläre Biophysik (ICS-4), FZ Jülich, 52428 Jülich, Germany, and.
Vladimir TodorovLaboratory for Experimental Nephrology, Division of Nephrology, University Hospital Dresden, 01307 Dresden Germany.
Daria GusevaFrom the Institut für Neurophysiologie, Medizinische Hochschule Hannover, 30625 Hannover, Germany.
Evgeni PonimaskinFrom the Institut für Neurophysiologie, Medizinische Hochschule Hannover, 30625 Hannover, Germany.
Christoph FahlkeInstitute of Complex Systems, Zelluläre Biophysik (ICS-4), FZ Jülich, 52428 Jülich, Germany, and c.fahlke@fz-juelich.de.
Martin FischerFrom the Institut für Neurophysiologie, Medizinische Hochschule Hannover, 30625 Hannover, Germany, fischer.martin@mh-hannover.de.
Medizinische Hochschule Hannover · DEForschungszentrum Jülich · DEUniversity Hospital Carl Gustav Carus · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CLC-K/barttin chloride channels are essential for NaCl re-absorption in Henle's loop and for potassium secretion by the stria vascularis in the inner ear. Here, we studied the posttranslational modification of such channels by palmitoylation of their accessory subunit barttin. We found that barttin is palmitoylated in vivo and in vitro and identified two conserved cysteine residues at positions 54 and 56 as palmitoylation sites. Point mutations at these two residues reduce the macroscopic current amplitudes in cells expressing CLC-K/barttin channels proportionally to the relative reduction in palmitoylated barttin. CLC-K/barttin expression, plasma membrane insertion, and single channel properties remain unaffected, indicating that these mutations decrease the number of active channels. R8W and G47R, two naturally occurring barttin mutations identified in patients with Bartter syndrome type IV, reduce barttin palmitoylation and CLC-K/barttin channel activity. Palmitoylation of the accessory subunit barttin might thus play a role in chloride channel dysfunction in certain variants of Bartter syndrome. We did not observe pronounced alteration of barttin palmitoylation upon increased salt and water intake or water deprivation, indicating that this posttranslational modification does not contribute to long term adaptation to variable water intake. Our results identify barttin palmitoylation as a novel posttranslational modification of CLC-K/barttin chloride channels.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsBartter SyndromeChloride ChannelsCysteineDogsHearing Loss, SensorineuralHEK293 CellsHumansLipoylationMadin Darby Canine Kidney CellsMolecular Sequence DataMutagenesis, Site-DirectedMutant ProteinsPoint MutationBSND protein, humanChloride ChannelsCLCNKA protein, humanCLCNKB protein, humanCysteineMutant ProteinsProtein SubunitsRecombinant Proteinsbarttinchloride channelelectrophysiologygatingintracellular traffickingpost-translational modification (PTM)protein palmitoylationrenal physiology

Identifiers

PMID26013830
PMCPMC4498076
OpenAlexW1783849468

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.