Evidence map›Paper›PMID 32641494›Full record

ArticleThe Journal of biological chemistry2020

Modulation of Kv4.2/KChIP3 interaction by the ceroid lipofuscinosis neuronal 3 protein CLN3.

Carolin Seifert, Stephan Storch, Robert Bähring

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.8field-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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Unifying biology of neurodegeneration in lysosomal storage diseases.Journal of inherited metabolic disease · 2025
    Review
  2. R-type voltage-gated CaCell reports · 2022
    Article
  3. Article
  4. 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

3 authors at 3 institutions in 1 country.

Carolin SeifertInstitut für Zelluläre und Integrative Physiologie, Zentrum für Experimentelle Medizin, Universitätsklinikum Hamburg-Eppendorf, Hamburg, Germany.
Stephan StorchKlinik und Poliklinik für Kinder- und Jugendmedizin, Pädiatrische Forschung, Universitätsklinikum Hamburg-Eppendorf, Hamburg, Germany.
Robert BähringInstitut für Zelluläre und Integrative Physiologie, Zentrum für Experimentelle Medizin, Universitätsklinikum Hamburg-Eppendorf, Hamburg, Germany. Electronic address: r.baehring@uke.de.
Klinik und Poliklinik für Kinder- und Jugendmedizin · DEUniversität Hamburg · DEUniversity Medical Center Hamburg-Eppendorf · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Voltage-gated potassium (Kv) channels of the Kv4 subfamily associate with Kv channel-interacting proteins (KChIPs), which leads to enhanced surface expression and shapes the inactivation gating of these channels. KChIP3 has been reported to also interact with the late endosomal/lysosomal membrane glycoprotein CLN3 (ceroid lipofuscinosis neuronal 3), which is modified because of gene mutation in juvenile neuronal ceroid lipofuscinosis (JNCL). The present study was undertaken to find out whether and how CLN3, by its interaction with KChIP3, may indirectly modulate Kv4.2 channel expression and function. To this end, we expressed KChIP3 and CLN3, either individually or simultaneously, together with Kv4.2 in HEK 293 cells. We performed co-immunoprecipitation experiments and found a lower amount of KChIP3 bound to Kv4.2 in the presence of CLN3. In whole-cell patch-clamp experiments, we examined the effects of CLN3 co-expression on the KChIP3-mediated modulation of Kv4.2 channels. Simultaneous co-expression of CLN3 and KChIP3 with Kv4.2 resulted in a suppression of the typical KChIP3-mediated modulation;

Indexed as

Kv Channel-Interacting ProteinsMembrane GlycoproteinsMolecular ChaperonesMutation, MissenseNeuronal Ceroid-LipofuscinosesRepressor ProteinsShal Potassium ChannelsAmino Acid SubstitutionGene Expression RegulationHEK293 CellsHumansProtein BindingCLN3 protein, humanKCNIP3 protein, humanKv Channel-Interacting ProteinsMembrane GlycoproteinsMolecular ChaperonesRepressor ProteinsShal Potassium ChannelsBatten diseasebiophysicscalciumgatingjuvenile neuronal ceroid lipofuscinosis (JNCL)KChIPKv channel-interacting proteinneurodegenerative diseasepatch–clamppotassium channelprotein complex

Identifiers

PMID32641494
PMCPMC7443505
OpenAlexW3041891565

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.