Evidence map›Paper›PMID 42030101›Full record

ArticleThe Journal of general physiology2026

Calmodulinopathy variants impair CaV1.3 and CaV2.1 regulation.

John W Hussey, Emily DeMarco, Deborah DiSilvestre, Malene Brohus, Ana-Octavia Busuioc, Emil D Iversen, Helene H Jensen, Mette Nyegaard, Michael T Overgaard, Manu Ben-Johny and 1 more

Abstract read
In one paragraph

Article in The Journal of general physiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors.

John W HusseyDepartment of Pharmacology and Physiology, University of Maryland School of Medicine, Baltimore, MD, USA.ORCID 0000-0002-1357-747X
Emily DeMarcoDepartment of Pharmacology and Physiology, University of Maryland School of Medicine, Baltimore, MD, USA.ORCID 0000-0002-4177-0664
Deborah DiSilvestreDepartment of Pharmacology and Physiology, University of Maryland School of Medicine, Baltimore, MD, USA.ORCID 0000-0002-2327-4472
Malene BrohusDepartment of Chemistry and Bioscience, Aalborg University, Aalborg, Denmark.ORCID 0000-0001-9247-8551
Ana-Octavia BusuiocDepartment of Chemistry and Bioscience, Aalborg University, Aalborg, Denmark.ORCID 0009-0009-4004-4319
Emil D IversenDepartment of Chemistry and Bioscience, Aalborg University, Aalborg, Denmark.ORCID 0009-0000-0366-2673
Helene H JensenDepartment of Chemistry and Bioscience, Aalborg University, Aalborg, Denmark.ORCID 0000-0002-8426-9802
Mette NyegaardDepartment of Health Science and Technology, Aalborg University, Aalborg, Denmark.ORCID 0000-0003-4973-8543
Michael T OvergaardDepartment of Chemistry and Bioscience, Aalborg University, Aalborg, Denmark.ORCID 0000-0002-1423-2481
Manu Ben-JohnyDepartment of Physiology and Cellular Biophysics, Columbia University, New York, NY, USA.ORCID 0000-0002-5645-0815
Ivy E DickDepartment of Pharmacology and Physiology, University of Maryland School of Medicine, Baltimore, MD, USA.ORCID 0000-0002-7253-6846

Funding

Next-generation calcium channel modulatorsR01HL149926 · NHLBI · UNIVERSITY OF MARYLAND BALTIMORE · PI Ivy E Dick · 2020 to 2026
$3.4M
Expanding the Pathogenic Mechanisms of CalmodulinopathiesR21NS127294 · NINDS · UNIVERSITY OF MARYLAND BALTIMORE · PI DICK, IVY E · 2022 to 2023
$425k
National Heart Lung and Blood Institute R01HL149926National Institutes of Neurological Disorders and Stroke R21NS127294NHLBI NIH HHS R01 HL149926NINDS NIH HHS R21 NS127294
6 · The paper itself

Abstract

Calmodulinopathies are caused by mutations in calmodulin (CaM) and result in debilitating cardiac arrythmias such as long-QT syndrome (LQTS) and catecholaminergic polymorphic ventricular tachycardia (CPVT). In addition, many patients exhibit neurological comorbidities, including developmental delay and autism spectrum disorder. Prior studies have identified the impairment of Ca2+/CaM-dependent inactivation (CDI) of CaV1.2 channels as a major pathogenic mechanism leading to the LQTS phenotype in these patients. However, the impact of these mutations on other voltage-gated calcium channels (VGCCs) has yet to be fully explored. Here, we examine the potential for pathological CaM variants to impair the Ca2+/CaM-dependent regulation of CaV1.3 and CaV2.1, both essential for neuronal function. We find that pathogenic mutations in CaM can impair the CDI of CaV1.3, with overlapping yet distinct disruption of the Ca2+-dependent facilitation (CDF) of CaV2.1 channels. Moreover, while the majority of CaM variants demonstrated the ability to bind the IQ region of each channel, differences were noted between CaV1.3 and CaV2.1, demonstrating unique CaM interactions across the two channel subtypes. Further, C-lobe CaM variants display a reduced ability to sense Ca2+ when in complex with the CaV IQ domains, explaining the Ca2+/CaM regulation deficits. Overall, these results support the possibility that disrupted Ca2+/CaM regulation of multiple VGCCs may contribute to the pathogenesis of calmodulinopathies.

Indexed as

Calcium Channels, L-TypeCalcium Channels, N-TypeCalmodulinAnimalsCalciumCaveolin 3HEK293 CellsHumansLong QT SyndromeMutationCalciumCalcium Channels, L-TypeCalcium Channels, N-TypeCalmodulinCAV3 protein, humanCaveolin 3

Identifiers

PMID42030101
PMCPMC13660674

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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.