Evidence map›Paper›PMID 18845608›Full record

ReviewThe Journal of physiology2008

Weighing the evidence for a ternary protein complex mediating A-type K+ currents in neurons.

Jonathon Maffie, Bernardo Rudy

Open access · greenAbstract readReview
In one paragraph

Review in The Journal of physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

67 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. KvThe Journal of physiology · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Castration Induces Down-Regulation of A-Type KInternational journal of molecular sciences · 2019
    Article
  10. Identification of IQM-266, a Novel DREAM Ligand That Modulates KFrontiers in molecular neuroscience · 2019
    Article
  11. Review
  12. A-Type KFrontiers in molecular neuroscience · 2018
    Review
  13. Article
  14. Review
  15. KThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

7 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 at 1 institution in 1 country.

Jonathon MaffieSmilow Neuroscience Program, Department of Physiology and Neuroscience, New York University School of Medicine, Smilow Research Center, 522 First Avenue, 6th Floor, New York, NY 10016, USA.
Bernardo Rudy
New York University · US

Funding

Molecular Components of A-type K+ ChannelsR01NS045217 · NINDS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI RUDY, BERNARDO · 2003 to 2013
$4.6M
NINDS NIH HHS NS 045217NINDS NIH HHS R01 NS045217
6 · The paper itself

Abstract

The subthreshold-operating A-type K(+) current in neurons (I(SA)) has important roles in the regulation of neuronal excitability, the timing of action potential firing and synaptic integration and plasticity. The channels mediating this current (Kv4 channels) have been implicated in epilepsy, the control of dopamine release, and the regulation of pain plasticity. It has been proposed that Kv4 channels in neurons are ternary complexes of three types of protein: pore forming subunits of the Kv4 subfamily and two types of auxiliary subunits, the Ca(2+) binding proteins KChIPs and the dipeptidyl peptidase-like proteins (DPPLs) DPP6 (also known as DPPX) and DPP10 (4 molecules of each per channel for a total of 12 proteins in the complex). Here we consider the evidence supporting this hypothesis. Kv4 channels in many neurons are likely to be ternary complexes of these three types of protein. KChIPs and DPPLs are required to efficiently traffic Kv4 channels to the plasma membrane and regulate the functional properties of the channels. These proteins may also be important in determining the localization of the channels to specific neuronal compartments, their dynamics, and their response to neuromodulators. A surprisingly large number of additional proteins have been shown to modify Kv4 channels in heterologous expression systems, but their association with native Kv4 channels in neurons has not been properly validated. A critical consideration of the evidence suggests that it is unlikely that association of Kv4 channels with these additional proteins is widespread in the CNS. However, we cannot exclude that some of these proteins may associate with the channels transiently or in specific neurons or neuronal compartments, or that they may associate with the channels in other tissues.

Indexed as

AnimalsHumansIon Channel GatingKv Channel-Interacting ProteinsModels, MolecularMultiprotein ComplexesNeuronsProtein BindingProtein Structure, TertiaryShal Potassium ChannelsKv Channel-Interacting ProteinsMultiprotein ComplexesShal Potassium Channels

Identifiers

PMID18845608
PMCPMC2655395
OpenAlexW1748649333

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.