Evidence map›Paper›PMID 40457251›Full record

ArticleCell communication and signaling : CCS2025

A subset of Orai1α and Orai1β subunits heteromerizes to form CRAC channels.

Jose J Lopez, Isaac Jardín, Vanesa Jiménez-Velarde, Sandra Alvarado, Alvaro Macías-Díaz, Joel Nieto-Felipe, Francisco J Martín-Romero, Tarik Smani, Juan A Rosado

Abstract read
In one paragraph

Article in Cell communication and signaling : CCS, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. Review
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

9 authors.

Jose J Lopez *Department of Physiology (Cellular Physiology Research Group), Institute of Molecular Pathology Biomarkers (IMPB), Universidad de Extremadura, Caceres, 10003, Spain.
Isaac Jardín *Department of Physiology (Cellular Physiology Research Group), Institute of Molecular Pathology Biomarkers (IMPB), Universidad de Extremadura, Caceres, 10003, Spain.
Vanesa Jiménez-VelardeDepartment of Physiology (Cellular Physiology Research Group), Institute of Molecular Pathology Biomarkers (IMPB), Universidad de Extremadura, Caceres, 10003, Spain.
Sandra AlvaradoDepartment of Physiology (Cellular Physiology Research Group), Institute of Molecular Pathology Biomarkers (IMPB), Universidad de Extremadura, Caceres, 10003, Spain.
Alvaro Macías-DíazDepartment of Physiology (Cellular Physiology Research Group), Institute of Molecular Pathology Biomarkers (IMPB), Universidad de Extremadura, Caceres, 10003, Spain.
Joel Nieto-FelipeDepartment of Physiology (Cellular Physiology Research Group), Institute of Molecular Pathology Biomarkers (IMPB), Universidad de Extremadura, Caceres, 10003, Spain.
Francisco J Martín-RomeroDepartment of Biochemistry and Molecular Biology, Institute of Molecular Pathology Biomarkers (IMPB), Universidad de Extremadura, Badajoz, 06006, Spain.
Tarik SmaniGroup of Cardiovascular Pathophysiology, Institute of Biomedicine of Seville, University Hospital of Virgen del Rocío/University of Seville/CSIC, Avenida Manuel Siurot s/n, Seville, 41013, Spain. tasmani@us.es.ORCID http://orcid.org/0000-0002-1877-7438
Juan A RosadoDepartment of Physiology (Cellular Physiology Research Group), Institute of Molecular Pathology Biomarkers (IMPB), Universidad de Extremadura, Caceres, 10003, Spain. jarosado@unex.es.ORCID http://orcid.org/0000-0002-9749-2325

Funding

Agencia Estatal de Investigación PID2022-136279NB-C21Agencia Estatal de Investigación PID2022-136279NB-C22Junta de Extremadura IB20007
6 · The paper itself

Abstract

backgroundCa

methodsA lipid raft isolation protocol in combination with Western blotting assay was conducted to detect the expression of each Orai1 variants in the isolated membrane fractions. Ca

resultsOur results indicate that Orai1α and Orai1β exhibit different lipid raft partitioning in resting cells when expressed individually, likely attributed to the presence of a caveolin-binding domain in Orai1α. However, when both variants are co-expressed, they show a similar distribution predominantly in the lipid raft domains, indicating potential interaction between the two Orai1 forms. Expression of a dominant-negative Orai1β mutant has been found to interfere with Orai1α-mediated Ca

conclusionsOur results indicate that while Orai1α and Orai1β mostly form separate CRAC channels, a small subset of both Orai1 variants combine to form heteromeric channels. These findings provide new insights on the nature of CRAC channels.

Indexed as

Calcium Release Activated Calcium ChannelsORAI1 ProteinProtein MultimerizationProtein SubunitsCalciumHEK293 CellsHumansMembrane MicrodomainsCalciumCalcium Release Activated Calcium ChannelsORAI1 ProteinORAI1 protein, humanProtein SubunitsLipid raftsOrai1αOrai1βStore-operated Ca2+ entry

Identifiers

PMID40457251
PMCPMC12131441

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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.