Evidence map›Paper›PMID 29937349›Full record

ArticleCurrent biology : CB2018

Electrostatic Tuning of a Potassium Channel in Electric Fish.

Immani Swapna, Alfredo Ghezzi, Julia M York, Michael R Markham, D Brent Halling, Ying Lu, Jason R Gallant, Harold H Zakon

Abstract read
In one paragraph

Article in Current biology : CB, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
–field-weighted citation impact
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

21 citing papers in PubMed.

  1. Electrostatic tuning of NaThe Journal of physiology · 2026
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  11. Review
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  14. Review
  15. Article
  16. Ontogeny of electric organ and electric organ discharge in Campylomormyrus rhynchophorus (Teleostei: Mormyridae).Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2020
    Article
  17. Review
  18. Article
  19. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Immani SwapnaDepartment of Neuroscience, The University of Texas at Austin, Austin, TX 78712, USA; Department of Integrative Biology, The University of Texas at Austin, Austin, TX 78712, USA.
Alfredo GhezziDepartment of Neuroscience, The University of Texas at Austin, Austin, TX 78712, USA; Department of Biology, University of Puerto Rico - Rio Piedras, San Juan, PR 00931, USA.
Julia M YorkDepartment of Integrative Biology, The University of Texas at Austin, Austin, TX 78712, USA.
Michael R MarkhamDepartment of Biology, The University of Oklahoma, Norman, OK 73019, USA.
D Brent HallingDepartment of Neuroscience, The University of Texas at Austin, Austin, TX 78712, USA.
Ying LuDepartment of Neuroscience, The University of Texas at Austin, Austin, TX 78712, USA.
Jason R GallantDepartment of Integrative Biology, Michigan State University, East Lansing, MI 48864, USA. Electronic address: jgallant@msu.edu.
Harold H ZakonDepartment of Neuroscience, The University of Texas at Austin, Austin, TX 78712, USA; Department of Integrative Biology, The University of Texas at Austin, Austin, TX 78712, USA. Electronic address: h.zakon@austin.utexas.edu.

Funding

Mechanisms of Calcium-Calmodulin Mediated Ion Channel GatingR01NS077821 · NINDS · UNIVERSITY OF TEXAS AT AUSTIN · PI ALDRICH, RICHARD · 2011 to 2021
$4.7M
State Dependent Affinity of Calmodulin for SK2F32GM093626 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI HALLING, DAVID BRENT · 2011 to 2012
$81k
NIGMS NIH HHS F32 GM093626NINDS NIH HHS R01 NS077821
6 · The paper itself

Abstract

Molecular variation contributes to the evolution of adaptive phenotypes, though it is often difficult to understand precisely how. The adaptively significant electric organ discharge behavior of weakly electric fish is the direct result of biophysical membrane properties set by ion channels. Here, we describe a voltage-gated potassium-channel gene in African electric fishes that is under positive selection and highly expressed in the electric organ. The channel produced by this gene shortens electric organ action potentials by activating quickly and at hyperpolarized membrane potentials. The source of these properties is a derived patch of negatively charged amino acids in an extracellular loop near the voltage sensor. We demonstrate that this negative patch acts by contributing to the global surface charge rather than by local interactions with specific amino acids in the channel's extracellular face. We suggest a more widespread role for this loop in the evolutionary tuning of voltage-dependent channels.

Indexed as

AnimalsElectric FishElectric OrganFish ProteinsGene ExpressionIon Channel GatingMembrane PotentialsPotassium Channels, Voltage-GatedSelection, GeneticFish ProteinsPotassium Channels, Voltage-Gatedbiophysicselectric fishelectric organevolutionkv1.7membrane surface chargemormyridpotassium channelRNA-seq

Identifiers

PMID29937349
PMCPMC6067922

What OpenQuestion holds

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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.