Evidence map›Paper›PMID 21118809›Full record

ArticleThe Journal of biological chemistry2011

KCNE4 juxtamembrane region is required for interaction with calmodulin and for functional suppression of KCNQ1.

Erin J Ciampa, Richard C Welch, Carlos G Vanoye, Alfred L George

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.5field-weighted citation impact, top 16% 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

25 citing papers in PubMed, 32 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Erin J CiampaDepartment of Pharmacology, Vanderbilt University, Nashville, Tennessee 37232, USA.
Richard C Welch
Carlos G Vanoye
Alfred L George
Vanderbilt University · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007347 · NIGMS · VANDERBILT UNIVERSITY · PI WILLIAMS, CHRISTOPHER S. · 1985 to 2023
$26.3M
Molecular Physiology of KCNE Potassium Channel SubunitsR01HL077188 · NHLBI · VANDERBILT UNIVERSITY · PI GEORGE, ALFRED L. · 2005 to 2008
$1.5M
NHLBI NIH HHS HL077188NHLBI NIH HHS R01 HL077188NIGMS NIH HHS T32 GM007347NIGMS NIH HHS T32 GM07347
6 · The paper itself

Abstract

Voltage-gated potassium (K(V)) channels, such as KCNQ1 (K(V)7.1), are modulated by accessory subunits and regulated by intracellular second messengers. Accessory subunits belonging to the KCNE family exert diverse functional effects on KCNQ1, have been implicated in the pathogenesis of various genetic disorders of heart rhythm, and contribute to transducing intracellular signaling events into changes in K(V) channel activity. We investigated the interactions between calmodulin (CaM), the ubiquitous Ca(2+)-transducing protein that binds and confers Ca(2+) sensitivity to the biophysical properties of KCNQ1, and KCNE4. These studies were motivated by the observed similarities between the suppression of KCNQ1 function by pharmacological disruption of KCNQ1-CaM interactions and the effects of KCNE4 co-expression on the channel. We determined that KCNE4, but not KCNE1, can biochemically interact with CaM and that this interaction is Ca(2+)-dependent and requires a tetraleucine motif in the juxtamembrane region of the KCNE4 C terminus. Furthermore, disruption of the KCNE4-CaM interaction either by mutagenesis of the tetraleucine motif or by acute Ca(2+) chelation impairs the ability of KCNE4 to inhibit KCNQ1. Our findings have potential relevance to KCNQ1 regulation both by KCNE accessory subunits and by an important intracellular signaling molecule.

Indexed as

Amino Acid MotifsAnimalsCalciumCalmodulinCHO CellsCricetinaeCricetulusGene Expression RegulationHumansKCNQ1 Potassium ChannelPotassium Channels, Voltage-GatedCalciumCalmodulinKCNE4 protein, humanKCNQ1 Potassium ChannelKCNQ1 protein, humanPotassium Channels, Voltage-Gated

Identifiers

PMID21118809
PMCPMC3039368
OpenAlexW1965325268

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.