Evidence map›Paper›PMID 34234241›Full record

ArticleScientific reports2021

Calmodulin-dependent KCNE4 dimerization controls membrane targeting.

Sara R Roig, Laura Solé, Silvia Cassinelli, Magalí Colomer-Molera, Daniel Sastre, Clara Serrano-Novillo, Antonio Serrano-Albarrás, M Pilar Lillo, Michael M Tamkun, Antonio Felipe

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

9 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Review
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  6. Nile Tilapia (International journal of molecular sciences · 2024
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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

10 authors at 4 institutions in 3 countries.

Sara R RoigMolecular Physiology Laboratory, Dpt. de Bioquímica I Biomedicina Molecular, Institut de Biomedicina (IBUB), Universitat de Barcelona, Avda. Diagonal 643, 08028, Barcelona, Spain.
Laura SoléMolecular Physiology Laboratory, Dpt. de Bioquímica I Biomedicina Molecular, Institut de Biomedicina (IBUB), Universitat de Barcelona, Avda. Diagonal 643, 08028, Barcelona, Spain.
Silvia CassinelliMolecular Physiology Laboratory, Dpt. de Bioquímica I Biomedicina Molecular, Institut de Biomedicina (IBUB), Universitat de Barcelona, Avda. Diagonal 643, 08028, Barcelona, Spain.
Magalí Colomer-MoleraMolecular Physiology Laboratory, Dpt. de Bioquímica I Biomedicina Molecular, Institut de Biomedicina (IBUB), Universitat de Barcelona, Avda. Diagonal 643, 08028, Barcelona, Spain.
Daniel SastreMolecular Physiology Laboratory, Dpt. de Bioquímica I Biomedicina Molecular, Institut de Biomedicina (IBUB), Universitat de Barcelona, Avda. Diagonal 643, 08028, Barcelona, Spain.
Clara Serrano-NovilloMolecular Physiology Laboratory, Dpt. de Bioquímica I Biomedicina Molecular, Institut de Biomedicina (IBUB), Universitat de Barcelona, Avda. Diagonal 643, 08028, Barcelona, Spain.
Antonio Serrano-AlbarrásMolecular Physiology Laboratory, Dpt. de Bioquímica I Biomedicina Molecular, Institut de Biomedicina (IBUB), Universitat de Barcelona, Avda. Diagonal 643, 08028, Barcelona, Spain.
M Pilar LilloInstituto de Química Física Rocasolano, CSIC, 28006, Madrid, Spain.
Michael M TamkunDepartment of Biomedical Sciences, Colorado State University, Fort Collins, CO, 80523, USA.
Antonio FelipeMolecular Physiology Laboratory, Dpt. de Bioquímica I Biomedicina Molecular, Institut de Biomedicina (IBUB), Universitat de Barcelona, Avda. Diagonal 643, 08028, Barcelona, Spain. afelipe@ub.edu.
Universitat de Barcelona · ESColorado State University · USInstituto de Química Física Blas Cabrera · ESUniversity of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The voltage-dependent potassium channel Kv1.3 participates in the immune response. Kv1.3 is essential in different cellular functions, such as proliferation, activation and apoptosis. Because aberrant expression of Kv1.3 is linked to autoimmune diseases, fine-tuning its function is crucial for leukocyte physiology. Regulatory KCNE subunits are expressed in the immune system, and KCNE4 specifically tightly regulates Kv1.3. KCNE4 modulates Kv1.3 currents slowing activation, accelerating inactivation and retaining the channel at the endoplasmic reticulum (ER), thereby altering its membrane localization. In addition, KCNE4 genomic variants are associated with immune pathologies. Therefore, an in-depth knowledge of KCNE4 function is extremely relevant for understanding immune system physiology. We demonstrate that KCNE4 dimerizes, which is unique among KCNE regulatory peptide family members. Furthermore, the juxtamembrane tetraleucine carboxyl-terminal domain of KCNE4 is a structural platform in which Kv1.3, Ca

Indexed as

Protein MultimerizationAmino Acid MotifsAmino Acid SequenceAnimalsCalmodulinCell MembraneElectrophysiological PhenomenaGene ExpressionHEK293 CellsHumansIon Channel GatingKv1.3 Potassium ChannelLeukocytesModels, BiologicalOrgan SpecificityPotassium Channels, Voltage-GatedCalmodulinKCNE4 protein, humanKv1.3 Potassium ChannelPotassium Channels, Voltage-Gated

Identifiers

PMID34234241
PMCPMC8263776
OpenAlexW3178237397

What OpenQuestion holds

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Registered trials

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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.