Evidence map›Paper›PMID 19279261›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2009

The dipeptidyl-peptidase-like protein DPP6 determines the unitary conductance of neuronal Kv4.2 channels.

Yuri A Kaulin, José A De Santiago-Castillo, Carmen A Rocha, Marcela S Nadal, Bernardo Rudy, Manuel Covarrubias

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

35 citing papers in PubMed, 47 citations in OpenAlex.

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  18. A-Type KFrontiers in molecular neuroscience · 2018
    Review
  19. Transmural gradients in ion channel and auxiliary subunit expression.Progress in biophysics and molecular biology · 2016
    Review
  20. Pore size matters for potassium channel conductance.The Journal of general physiology · 2016
    Review
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

6 authors at 2 institutions in 1 country.

Yuri A KaulinDepartment of Pathology, Anatomy, and Cell Biology, Jefferson Medical College of Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA. yuri.kaulin@jefferson.edu
José A De Santiago-Castillo
Carmen A Rocha
Marcela S Nadal
Bernardo Rudy
Manuel Covarrubias
Thomas Jefferson University · USNew York University · US

Funding

EXPRESSION AND FUNCTION OF K+ CHANNEL GENES IN THE CNSR01NS030989 · NINDS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI RUDY, BERNARDO · 1992 to 2015
$6.3M
Molecular Components of A-type K+ ChannelsR01NS045217 · NINDS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI RUDY, BERNARDO · 2003 to 2013
$4.6M
MOLECULAR PROPERTIES OF SUBTHRESHOLD POTASSIUM CHANNELSR01NS032337 · NINDS · THOMAS JEFFERSON UNIVERSITY · PI COVARRUBIAS, MANUEL L · 1999 to 2010
$2.8M
NINDS NIH HHS NS045217NINDS NIH HHS NS30989NINDS NIH HHS R01 NS030989NINDS NIH HHS R01 NS032337NINDS NIH HHS R01 NS032337-13NINDS NIH HHS R01 NS045217
6 · The paper itself

Abstract

The neuronal subthreshold-operating A-type K(+) current regulates electrical excitability, spike timing, and synaptic integration and plasticity. The Kv4 channels underlying this current have been implicated in epilepsy, regulation of dopamine release, and pain plasticity. However, the unitary conductance (gamma) of neuronal somatodendritic A-type K(+) channels composed of Kv4 pore-forming subunits is larger (approximately 7.5 pS) than that of Kv4 channels expressed singly in heterologous cells (approximately 4 pS). Here, we examined the putative novel contribution of the dipeptidyl-peptidase-like protein-6 DPP6-S to the gamma of native [cerebellar granule neuron (CGN)] and reconstituted Kv4.2 channels. Coexpression of Kv4.2 proteins with DPP6-S was sufficient to match the gamma of native CGN channels; and CGN Kv4 channels from dpp6 knock-out mice yielded a gamma indistinguishable from that of Kv4.2 channels expressed singly. Moreover, suggesting electrostatic interactions, charge neutralization mutations of two N-terminal acidic residues in DPP6-S eliminated the increase in gamma. Therefore, DPP6-S, as a membrane protein extrinsic to the pore domain, is necessary and sufficient to explain a fundamental difference between native and recombinant Kv4 channels. These observations may help to understand the molecular basis of neurological disorders correlated with recently identified human mutations in the dpp6 gene.

Indexed as

AnimalsDipeptidyl-Peptidases and Tripeptidyl-PeptidasesFemaleMembrane PotentialsMiceMice, KnockoutNerve Tissue ProteinsNeuronsPeptide HydrolasesPotassium ChannelsRatsShal Potassium ChannelsXenopus laevisDipeptidyl-Peptidases and Tripeptidyl-PeptidasesDPP6 protein, humanNerve Tissue ProteinsPeptide HydrolasesPotassium ChannelsShal Potassium Channels

Identifiers

PMID19279261
PMCPMC3758885
OpenAlexW2049764845

What OpenQuestion holds

Textmetadata
LicenceTDM
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.