Evidence map›Paper›PMID 16908725›Full record

ArticleThe Journal of general physiology2006

Molecular template for a voltage sensor in a novel K+ channel. I. Identification and functional characterization of KvLm, a voltage-gated K+ channel from Listeria monocytogenes.

Jose S Santos, Alicia Lundby, Cecilia Zazueta, Mauricio Montal

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

19 citing papers in PubMed, 26 citations in OpenAlex.

  1. Modular architecture of KEMBO reports · 2025
    Review
  2. Article
  3. Article
  4. Article
  5. From damage response to action potentials: early evolution of neural and contractile modules in stem eukaryotes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016
    Review
  6. Structure of potassium channels.Cellular and molecular life sciences : CMLS · 2015
    Review
  7. The application of theBiotechnology reports (Amsterdam, Netherlands) · 2015
    Article
  8. Lipid bilayer modules as determinants of K+ channel gating.The Journal of biological chemistry · 2014
    Article
  9. Review
  10. Article
  11. Tetrameric assembly of KvLm K+ channels with defined numbers of voltage sensors.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  12. Voltage-gated sodium channel (NaV) protein dissection creates a set of functional pore-only proteins.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  13. Article
  14. Article
  15. Ion channels in microbes.Physiological reviews · 2008
    Review
  16. Article
  17. Article
  18. Article
  19. 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

4 authors at 1 institution in 1 country.

Jose S SantosSection of Neurobiology, Division of Biological Sciences, University of California San Diego, La Jolla, CA 92093, USA.
Alicia Lundby
Cecilia Zazueta
Mauricio Montal
University of California, San Diego · US

Funding

NEUROBIOLOGY TRAINING PROGRAMT32NS007220 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI JIN, YISHI · 1985 to 2023
$4.5M
Modular Design of Voltage-Gated Channel ProteinsR01GM049711 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI MONTAL, MAURICIO S · 1993 to 2017
$4.2M
NIGMS NIH HHS R01 GM049711NIGMS NIH HHS R01-GM49711NINDS NIH HHS T32 NS007220NINDS NIH HHS T32-NS07220
6 · The paper itself

Abstract

The fundamental principles underlying voltage sensing, a hallmark feature of electrically excitable cells, are still enigmatic and the subject of intense scrutiny and controversy. Here we show that a novel prokaryotic voltage-gated K(+) (Kv) channel from Listeria monocytogenes (KvLm) embodies a rudimentary, yet robust, sensor sufficient to endow it with voltage-dependent features comparable to those of eukaryotic Kv channels. The most conspicuous feature of the KvLm sequence is the nature of the sensor components: the motif is recognizable; it appears, however, to contain only three out of eight charged residues known to be conserved in eukaryotic Kv channels and accepted to be deterministic for folding and sensing. Despite the atypical sensor sequence, flux assays of KvLm reconstituted in liposomes disclosed a channel pore that is highly selective for K(+) and is blocked by conventional Kv channel blockers. Single-channel currents recorded in symmetric K(+) solutions from patches of enlarged Escherichia coli (spheroplasts) expressing KvLm showed that channel open probability sharply increases with depolarization, a hallmark feature of Kv channels. The identification of a voltage sensor module in KvLm with a voltage dependence comparable to that of other eukaryotic Kv channels yet encoded by a sequence that departs significantly from the consensus sequence of a eukaryotic voltage sensor establishes a molecular blueprint of a minimal sequence for a voltage sensor.

Indexed as

Amino Acid SequenceAnimalsBacterial ProteinsDrosophilaGenome, BacterialIon Channel GatingListeria monocytogenesMembrane PotentialsMolecular Sequence DataPotassium ChannelsPotassium Channels, Voltage-GatedSequence AlignmentSpheroplastsBacterial ProteinsPotassium ChannelsPotassium Channels, Voltage-Gatedprokaryotic potassium channel

Identifiers

PMID16908725
PMCPMC2151562
OpenAlexW2071565003

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.