Evidence map›Paper›PMID 23692269›Full record

ArticleJournal of neurochemistry2013

Functional stoichiometry underlying KChIP regulation of Kv4.2 functional expression.

Kumud Kunjilwar, Yan Qian, Paul J Pfaffinger

Open access · greenAbstract read
In one paragraph

Article in Journal of neurochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.7field-weighted citation impact, top 28% 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

10 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Article
  3. R-type voltage-gated CaCell reports · 2022
    Article
  4. Article
  5. Article
  6. Sense and specificity in neuronal calcium signalling.Biochimica et biophysica acta · 2015
    Review
  7. Article
  8. Article
  9. The expression pattern of a Cav3-Kv4 complex differentially regulates spike output in cerebellar granule cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  10. 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

3 authors at 1 institution in 1 country.

Kumud KunjilwarDepartment of Neuroscience, Baylor College of Medicine, Houston, Texas 77030, USA.
Yan Qian
Paul J Pfaffinger
Baylor College of Medicine · US

Funding

UNDERSTANDING FXTAS AMONG MALES WITH THE FMR1 PREMUTATIONP30HD024064 · NICHD · BAYLOR COLLEGE OF MEDICINE · PI TOLIAS, KIMBERLY R · 1988 to 2013
$29.4M
Regulation of Neuronal Excitability (P01)P01NS037444 · NINDS · UNIVERSITY OF TEXAS AUSTIN · PI JOHNSTON, DANIEL · 1999 to 2008
$8.4M
FUNCTIONAL DOMAINS OF POTASSIUM CHANNEL SUBUNIT PROTEINSR01NS031583 · NINDS · BAYLOR COLLEGE OF MEDICINE · PI PFAFFINGER, PAUL · 1993 to 2004
$1.8M
A Current Regulation by Dipeptidyl Peptidase-Like ProteinsR01GM090029 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI PFAFFINGER, PAUL · 2010 to 2013
$1.2M
NICHD NIH HHS HD24064NICHD NIH HHS P30 HD024064NIGMS NIH HHS R01 GM090029NINDS NIH HHS P01 NS037444NINDS NIH HHS P01NS37444NINDS NIH HHS R01 NS031583NINDS NIH HHS R01NS31583
6 · The paper itself

Abstract

K channel-interacting proteins (KChIPs) enhance functional expression of Kv4 channels by binding to an N-terminal regulatory region located in the first 40 amino acids of Kv4.2 that we call the functional expression regulating N-terminal (FERN) domain. Mutating two residues in the FERN domain to alanines, W8A and F11A, disrupts KChIP binding and regulation of Kv4.2 without eliminating the FERN domain's control of basal expression level or regulation by DPP6. When Kv4.2(W8A,F11A) is co-expressed with wild type Kv4.2 and KChIP3 subunits, a dominant negative effect is seen where the current expression is reduced to levels normally seen without KChIP addition. The dominant negative effect correlates with heteromultimeric channels remaining on intracellular membranes despite KChIP binding to non-mutant Kv4.2 subunits. In contrast, the deletion mutant Kv4.2(Δ1-40), eliminating both KChIP binding and the FERN domain, has no dominant negative effect even though the maximal conductance level is 5x lower than seen with KChIP3. The 5x increased expression seen with KChIP integration into the channel is fully apparent even when a reduced number of KChIP subunits are incorporated as long as all FERN domains are bound. Our results support the hypothesis that KChIPs enhances Kv4.2 functional expression by a 1 : 1 suppression of the N-terminal FERN domain and by producing additional positive regulatory effects on functional channel expression.

Indexed as

AnimalsChlorocebus aethiopsCHO CellsCloning, MolecularCOS CellsCricetinaeGreen Fluorescent ProteinsIntracellular MembranesIon Channel GatingKv Channel-Interacting ProteinsMembrane PotentialsMutagenesisProtein BindingProtein Structure, TertiaryProtein SubunitsProtein TransportGreen Fluorescent ProteinsKCNIP3 protein, humanKv Channel-Interacting ProteinsProtein SubunitsRepressor ProteinsShal Potassium ChannelsA-currentauxiliary subunitdominant negativeKChIPKv4potassium channel

Identifiers

PMID23692269
PMCPMC3737270
OpenAlexW2094137857

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.