Evidence map›Paper›PMID 19623261›Full record

ArticlePloS one2009

KCNE1 and KCNE3 beta-subunits regulate membrane surface expression of Kv12.2 K(+) channels in vitro and form a tripartite complex in vivo.

Sinead M Clancy, Bihan Chen, Federica Bertaso, Julien Mamet, Timothy Jegla

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.9field-weighted citation impact, top 22% 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

16 citing papers in PubMed, 21 citations in OpenAlex.

  1. KCommunications medicine · 2026
    Article
  2. Review
  3. International journal of molecular sciences · 2025
    Article
  4. Article
  5. Kv12-Encoded KbioRxiv : the preprint server for biology · 2023
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. BACE1 and presenilin/γ-secretase regulate proteolytic processing of KCNE1 and 2, auxiliary subunits of voltage-gated potassium channels.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013
    Article
  12. Article
  13. Genetic dissection reveals unexpected influence of beta subunits on KCNQ1 K+ channel polarized trafficking in vivo.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011
    Article
  14. Article
  15. Article
  16. 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

5 authors at 1 institution in 1 country.

Sinead M ClancyDepartment of Cell Biology, Institute for Childhood and Neglected Diseases, The Scripps Research Institute, La Jolla, CA, USA.
Bihan Chen
Federica Bertaso
Julien Mamet
Timothy Jegla
Scripps Research Institute · US

Funding

Development of HTS Assays for Sub-Threshold Potassium ChannelsR21NS057000 · NINDS · SCRIPPS RESEARCH INSTITUTE, THE · PI JEGLA, TIMOTHY J · 2006 to 2006
$232k
NINDS NIH HHS R21 NS057000NINDS NIH HHS R21 NS057000I
6 · The paper itself

Abstract

Voltage-gated potassium channels that activate near the neuronal resting membrane potential are important regulators of excitation in the nervous system, but their functional diversity is still not well understood. For instance, Kv12.2 (ELK2, KCNH3) channels are highly expressed in the cerebral cortex and hippocampus, and although they are most likely to contribute to resting potassium conductance, surprisingly little is known about their function or regulation. Here we demonstrate that the auxiliary MinK (KCNE1) and MiRP2 (KCNE3) proteins are important regulators of Kv12.2 channel function. Reduction of endogenous KCNE1 or KCNE3 expression by siRNA silencing, significantly increased macroscopic Kv12.2 currents in Xenopus oocytes by around 4-fold. Interestingly, an almost 9-fold increase in Kv12.2 currents was observed with the dual injection of KCNE1 and KCNE3 siRNA, suggesting an additive effect. Consistent with these findings, over-expression of KCNE1 and/or KCNE3 suppressed Kv12.2 currents. Membrane surface biotinylation assays showed that surface expression of Kv12.2 was significantly increased by KCNE1 and KCNE3 siRNA, whereas total protein expression of Kv12.2 was not affected. KCNE1 and KCNE3 siRNA shifted the voltages for half-maximal activation to more hyperpolarized voltages, indicating that KCNE1 and KCNE3 may also inhibit activation gating of Kv12.2. Native co-immunoprecipitation assays from mouse brain membranes imply that KCNE1 and KCNE3 interact with Kv12.2 simultaneously in vivo, suggesting the existence of novel KCNE1-KCNE3-Kv12.2 channel tripartite complexes. Together these data indicate that KCNE1 and KCNE3 interact directly with Kv12.2 channels to regulate channel membrane trafficking.

Indexed as

Amino Acid SequenceAnimalsBase SequenceDNA PrimersEther-A-Go-Go Potassium ChannelsImmunoprecipitationIn Vitro TechniquesMembrane ProteinsMiceMolecular Sequence DataPatch-Clamp TechniquesPotassium Channels, Voltage-GatedRNA, Small InterferingSequence Homology, Amino AcidXenopusDNA PrimersEther-A-Go-Go Potassium ChannelsKcne1 protein, mouseKcne3 protein, mouseKcnh3 protein, mouseMembrane ProteinsPotassium Channels, Voltage-GatedRNA, Small Interfering

Identifiers

PMID19623261
PMCPMC2710002
OpenAlexW2046560280

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.