Evidence map›Paper›PMID 34196606›Full record

ArticleeLife2021

A novel mitochondrial Kv1.3-caveolin axis controls cell survival and apoptosis.

Jesusa Capera, Mireia Pérez-Verdaguer, Roberta Peruzzo, María Navarro-Pérez, Juan Martínez-Pinna, Armando Alberola-Die, Andrés Morales, Luigi Leanza, Ildiko Szabó, Antonio Felipe

Open access · goldAbstract read
In one paragraph

Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

18 citing papers in PubMed, 25 citations in OpenAlex.

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  9. [The peptide toxin components and nucleotide metabolites inNan fang yi ke da xue xue bao = Journal of Southern Medical University · 2025
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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 5 institutions in 4 countries.

Jesusa Capera *Molecular Physiology Laboratory, Dpt. de Bioquímica i Biomedicina Molecular, Institut de Biomedicina (IBUB), Universitat de Barcelona, Barcelona, Spain.ORCID 0000-0002-8123-7725
Mireia Pérez-Verdaguer *Molecular Physiology Laboratory, Dpt. de Bioquímica i Biomedicina Molecular, Institut de Biomedicina (IBUB), Universitat de Barcelona, Barcelona, Spain.
Roberta Peruzzo *Department of Biology, University of Padova, Padova, Italy.ORCID 0000-0001-9209-9068
María Navarro-Pérez *Molecular Physiology Laboratory, Dpt. de Bioquímica i Biomedicina Molecular, Institut de Biomedicina (IBUB), Universitat de Barcelona, Barcelona, Spain.ORCID 0000-0001-8106-9787
Juan Martínez-PinnaDept de Fisiología, Genética y Microbiología, Universidad de Alicante, Alicante, Spain.
Armando Alberola-DieDept de Fisiología, Genética y Microbiología, Universidad de Alicante, Alicante, Spain.ORCID 0000-0001-5391-5739
Andrés MoralesDept de Fisiología, Genética y Microbiología, Universidad de Alicante, Alicante, Spain.
Luigi LeanzaDepartment of Biology, University of Padova, Padova, Italy.
Ildiko SzabóDepartment of Biology, University of Padova, Padova, Italy.
Antonio FelipeMolecular Physiology Laboratory, Dpt. de Bioquímica i Biomedicina Molecular, Institut de Biomedicina (IBUB), Universitat de Barcelona, Barcelona, Spain.ORCID 0000-0002-7294-6431
University of Alicante · ESUniversity of Padua · ITUniversitat de Barcelona · ESUniversity of Oxford · GBUniversity of Pittsburgh · US

Funding

Italian Association for Cancer Research 20286Ministerio de Ciencia, Innovación y Universidades BFU2017-87104-RMinisterio de Ciencia, Innovación y Universidades CSD2008-00005Ministerio de Ciencia, Innovación y Universidades PID2020-112647RB-I00Ministero dell'Istruzione, dell'Università e della Ricerca PRIN 20174TB8KW_004
6 · The paper itself

Abstract

The voltage-gated potassium channel Kv1.3 plays an apparent dual physiological role by participating in activation and proliferation of leukocytes as well as promoting apoptosis in several types of tumor cells. Therefore, Kv1.3 is considered a potential pharmacological target for immunodeficiency and cancer. Different cellular locations of Kv1.3, at the plasma membrane or the mitochondria, could be responsible for such duality. While plasma membrane Kv1.3 facilitates proliferation, the mitochondrial channel modulates apoptotic signaling. Several molecular determinants of Kv1.3 drive the channel to the cell surface, but no information is available about its mitochondrial targeting. Caveolins, which are able to modulate cell survival, participate in the plasma membrane targeting of Kv1.3. The channel, via a caveolin-binding domain (CDB), associates with caveolin 1 (Cav1), which localizes Kv1.3 to lipid raft membrane microdomains. The aim of our study was to understand the role of such interactions not only for channel targeting but also for cell survival in mammalian cells. By using a caveolin association-deficient channel (Kv1.3 CDB

Indexed as

ApoptosisCaveolin 1Cell SurvivalHEK293 CellsHumansKv1.3 Potassium ChannelMitochondriaCAV1 protein, humanCaveolin 1KCNA3 protein, humanKv1.3 Potassium Channelapoptosiscancer biologycell biologyhumanion channelsleukocytesmousexenopus

Identifiers

PMID34196606
PMCPMC8248986
OpenAlexW3176701427

What Socratic 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 Socratic graph.