The molecular transition that confers voltage dependence to muscle contraction

Abstract What is the molecular origin of voltage dependence in skeletal muscle excitation-contraction? Cholinergic transmission to the muscle fiber triggers action potentials, which are sensed by voltage-gated L-type calcium channels (CaV1.1). In turn, the conformational changes in CaV1.1 propagate...

Full description

Saved in:
Bibliographic Details
Main Authors: Marina Angelini, Nicoletta Savalli, Federica Steccanella, Savana Maxfield, Serena Pozzi, Marino DiFranco, Stephen C. Cannon, Antonios Pantazis, Riccardo Olcese
Format: Article
Language:English
Published: Nature Portfolio 2025-05-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-025-59649-7
Tags: Add Tag
No Tags, Be the first to tag this record!
_version_ 1850269151407374336
author Marina Angelini
Nicoletta Savalli
Federica Steccanella
Savana Maxfield
Serena Pozzi
Marino DiFranco
Stephen C. Cannon
Antonios Pantazis
Riccardo Olcese
author_facet Marina Angelini
Nicoletta Savalli
Federica Steccanella
Savana Maxfield
Serena Pozzi
Marino DiFranco
Stephen C. Cannon
Antonios Pantazis
Riccardo Olcese
author_sort Marina Angelini
collection DOAJ
description Abstract What is the molecular origin of voltage dependence in skeletal muscle excitation-contraction? Cholinergic transmission to the muscle fiber triggers action potentials, which are sensed by voltage-gated L-type calcium channels (CaV1.1). In turn, the conformational changes in CaV1.1 propagate to and activate intracellular ryanodine receptors (RyR1), causing Ca2+ release and contraction. The CaV1.1 channel has four voltage-sensing domains (VSD-I to -IV) with diverse voltage-sensing properties, so the identity of VSD(s) responsible for conferring voltage dependence to RyR1 opening, is unknown. Using voltage-clamp fluorometry, we show that only VSD-III possesses kinetic, voltage-dependent and pharmacological properties consistent with skeletal-muscle excitability and Ca2+ release. We propose that the earliest voltage-dependent event in the excitation-contraction process is the structural rearrangement of VSD-III that propagates to RyR1 to initiate Ca2+ release and contraction.
format Article
id doaj-art-72f9196f117e4464a2ca49b0dc67225a
institution OA Journals
issn 2041-1723
language English
publishDate 2025-05-01
publisher Nature Portfolio
record_format Article
series Nature Communications
spelling doaj-art-72f9196f117e4464a2ca49b0dc67225a2025-08-20T01:53:14ZengNature PortfolioNature Communications2041-17232025-05-0116111010.1038/s41467-025-59649-7The molecular transition that confers voltage dependence to muscle contractionMarina Angelini0Nicoletta Savalli1Federica Steccanella2Savana Maxfield3Serena Pozzi4Marino DiFranco5Stephen C. Cannon6Antonios Pantazis7Riccardo Olcese8Division of Molecular Medicine, Department of Anesthesiology & Perioperative Medicine, David Geffen School of Medicine, University of California Los AngelesDivision of Molecular Medicine, Department of Anesthesiology & Perioperative Medicine, David Geffen School of Medicine, University of California Los AngelesDivision of Molecular Medicine, Department of Anesthesiology & Perioperative Medicine, David Geffen School of Medicine, University of California Los AngelesDivision of Molecular Medicine, Department of Anesthesiology & Perioperative Medicine, David Geffen School of Medicine, University of California Los AngelesDivision of Cell and Neurobiology, Department of Biomedical and Clinical Sciences, Linköping UniversityDepartment of Physiology, David Geffen School of Medicine, University of California Los AngelesDepartment of Physiology, David Geffen School of Medicine, University of California Los AngelesDivision of Cell and Neurobiology, Department of Biomedical and Clinical Sciences, Linköping UniversityDivision of Molecular Medicine, Department of Anesthesiology & Perioperative Medicine, David Geffen School of Medicine, University of California Los AngelesAbstract What is the molecular origin of voltage dependence in skeletal muscle excitation-contraction? Cholinergic transmission to the muscle fiber triggers action potentials, which are sensed by voltage-gated L-type calcium channels (CaV1.1). In turn, the conformational changes in CaV1.1 propagate to and activate intracellular ryanodine receptors (RyR1), causing Ca2+ release and contraction. The CaV1.1 channel has four voltage-sensing domains (VSD-I to -IV) with diverse voltage-sensing properties, so the identity of VSD(s) responsible for conferring voltage dependence to RyR1 opening, is unknown. Using voltage-clamp fluorometry, we show that only VSD-III possesses kinetic, voltage-dependent and pharmacological properties consistent with skeletal-muscle excitability and Ca2+ release. We propose that the earliest voltage-dependent event in the excitation-contraction process is the structural rearrangement of VSD-III that propagates to RyR1 to initiate Ca2+ release and contraction.https://doi.org/10.1038/s41467-025-59649-7
spellingShingle Marina Angelini
Nicoletta Savalli
Federica Steccanella
Savana Maxfield
Serena Pozzi
Marino DiFranco
Stephen C. Cannon
Antonios Pantazis
Riccardo Olcese
The molecular transition that confers voltage dependence to muscle contraction
Nature Communications
title The molecular transition that confers voltage dependence to muscle contraction
title_full The molecular transition that confers voltage dependence to muscle contraction
title_fullStr The molecular transition that confers voltage dependence to muscle contraction
title_full_unstemmed The molecular transition that confers voltage dependence to muscle contraction
title_short The molecular transition that confers voltage dependence to muscle contraction
title_sort molecular transition that confers voltage dependence to muscle contraction
url https://doi.org/10.1038/s41467-025-59649-7
work_keys_str_mv AT marinaangelini themoleculartransitionthatconfersvoltagedependencetomusclecontraction
AT nicolettasavalli themoleculartransitionthatconfersvoltagedependencetomusclecontraction
AT federicasteccanella themoleculartransitionthatconfersvoltagedependencetomusclecontraction
AT savanamaxfield themoleculartransitionthatconfersvoltagedependencetomusclecontraction
AT serenapozzi themoleculartransitionthatconfersvoltagedependencetomusclecontraction
AT marinodifranco themoleculartransitionthatconfersvoltagedependencetomusclecontraction
AT stephenccannon themoleculartransitionthatconfersvoltagedependencetomusclecontraction
AT antoniospantazis themoleculartransitionthatconfersvoltagedependencetomusclecontraction
AT riccardoolcese themoleculartransitionthatconfersvoltagedependencetomusclecontraction
AT marinaangelini moleculartransitionthatconfersvoltagedependencetomusclecontraction
AT nicolettasavalli moleculartransitionthatconfersvoltagedependencetomusclecontraction
AT federicasteccanella moleculartransitionthatconfersvoltagedependencetomusclecontraction
AT savanamaxfield moleculartransitionthatconfersvoltagedependencetomusclecontraction
AT serenapozzi moleculartransitionthatconfersvoltagedependencetomusclecontraction
AT marinodifranco moleculartransitionthatconfersvoltagedependencetomusclecontraction
AT stephenccannon moleculartransitionthatconfersvoltagedependencetomusclecontraction
AT antoniospantazis moleculartransitionthatconfersvoltagedependencetomusclecontraction
AT riccardoolcese moleculartransitionthatconfersvoltagedependencetomusclecontraction