Evidence map›Paper›PMID 16407566›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2006

The Kv2.1 C terminus can autonomously transfer Kv2.1-like phosphorylation-dependent localization, voltage-dependent gating, and muscarinic modulation to diverse Kv channels.

Durga P Mohapatra, James S Trimmer

Abstract readComparative Study
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing 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

71 citing papers in PubMed.

  1. Molecular contacts in self-assembling clusters of membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Glucocorticoids Rapidly Modulate CaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  3. Increased KCells · 2022
    Article
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  8. Kv2.1 channels play opposing roles in regulating membrane potential, CaProceedings of the National Academy of Sciences of the United States of America · 2020
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  9. Article
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  11. Article
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  13. Kv2 potassium channels form endoplasmic reticulum/plasma membrane junctions via interaction with VAPA and VAPB.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Article
  15. Article
  16. Disruption of KNeuroscience · 2017
    Article
  17. Chronic CaThe Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2017
    Article
  18. Article
  19. Article
  20. Article

11 more citing papers are in PubMed but not listed here.

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

2 authors.

Durga P MohapatraDepartment of Pharmacology, School of Medicine, University of California, Davis, California 95616, USA.
James S Trimmer

Funding

Transgenic Mouse and Biobank CoreP01CA095616 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI BRENNAN, CAMERON · 2003 to 2012
$20.3M
Determinants of Dendritic Potassium Channel LocalizationR01NS042225 · NINDS · UNIVERSITY OF CALIFORNIA DAVIS · PI TRIMMER, JAMES S · 2001 to 2014
$6.3M
NCI NIH HHS P01 CA095616NINDS NIH HHS NS42225NINDS NIH HHS R01 NS042225
6 · The paper itself

Abstract

Modulation of K+ channels is widely used to dynamically regulate neuronal membrane excitability. The voltage-gated K+ channel Kv2.1 is an abundant delayed rectifier K+ (IK) channel expressed at high levels in many types of mammalian central neurons where it regulates diverse aspects of membrane excitability. Neuronal Kv2.1 is constitutively phosphorylated, localized in high-density somatodendritic clusters, and has a relatively depolarized voltage dependence of activation. Here, we show that the clustering and voltage-dependent gating of endogenous Kv2.1 in cultured rat hippocampal neurons are modulated by cholinergic stimulation, a common form of neuromodulation. The properties of neuronal Kv2.1 are recapitulated in recombinant Kv2.1 expressed in human embryonic kidney 293 (HEK293) cells, but not COS-1 cells, because of cell background-specific differences in Kv2.1 phosphorylation. As in neurons, Kv2.1 in HEK293 cells is dynamically regulated by cholinergic stimulation, which leads to Ca2+/calcineurin-dependent dephosphorylation of Kv2.1, dispersion of channel clusters, and hyperpolarizing shifts in the voltage-dependent gating properties of the channel. Immunocytochemical, biochemical, and biophysical analyses of chimeric Kv channels show that the Kv2.1 cytoplasmic C-terminal domain can act as an autonomous domain sufficient to transfer Kv2.1-like clustering, voltage-dependent activation, and cholinergic modulation to diverse Kv channels. These findings provide novel mechanistic insights into cholinergic modulation of ion channels and regulation of the localization and voltage-dependent gating properties of the abundant neuronal Kv2.1 channel by cholinergic and other neuromodulatory stimuli.

Indexed as

AnimalsCalcineurinCalciumCarbacholCell LineCell MembraneCells, CulturedChlorocebus aethiopsCOS CellsElectrophoresis, Polyacrylamide GelHippocampusHumansIon Channel GatingIonomycinIon TransportKidneyCalcineurinCalciumCarbacholIonomycinKv1.5 Potassium ChannelMuscarinic AgonistsNerve Tissue ProteinsPotassiumReceptors, MuscarinicRecombinant Fusion ProteinsShab Potassium Channels

Identifiers

PMID16407566
PMCPMC6674430

What OpenQuestion holds

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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.