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A rich conformational palette underlies human CaV2.1-channel availability
Linköping University, Department of Biomedical and Clinical Sciences, The Division of Cell and Neurobiology. Linköping University, Faculty of Medicine and Health Sciences.ORCID iD: 0000-0002-6315-8732
Linköping University, Faculty of Medicine and Health Sciences. Linköping University, Department of Biomedical and Clinical Sciences, The Division of Cell and Neurobiology.ORCID iD: 0000-0002-0891-7732
Department of Anesthesiology and Perioperative Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA, USA.ORCID iD: 0000-0003-4621-3784
Department of Anesthesiology and Perioperative Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA, USA, and Department of Physiology, David Geffen School of Medicine, University of California, Los Angeles, CA, USA.ORCID iD: 0000-0003-4225-9814
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2025 (English)In: Nature Communications, E-ISSN 2041-1723, Vol. 16, no 1, article id 3815Article in journal (Refereed) Published
Abstract [en]

Depolarization-evoked opening of CaV2.1 (P/Q-type) Ca2+-channels triggers neurotransmitter release, while voltage-dependent inactivation (VDI) limits channel availability to open, contributing to synaptic plasticity. The mechanism of CaV2.1 response to voltage is unclear. Using voltage-clamp fluorometry and kinetic modeling, we optically track and physically characterize the structural dynamics of the four CaV2.1 voltage-sensor domains (VSDs). The VSDs are differentially sensitive to voltage changes, both brief and long-lived. VSD-I seems to directly drive opening and convert between two modes of function, associated with VDI. VSD-II is apparently voltage-insensitive. VSD-III and VSD-IV sense more negative voltages and undergo voltage-dependent conversion uncorrelated with VDI. Auxiliary β-subunits regulate VSD-I-to-pore coupling and VSD conversion kinetics. Hence, the central role of CaV2.1 channels in synaptic release, and their contribution to plasticity, memory formation and learning, can arise from the voltage-dependent conformational changes of VSD-I.

Place, publisher, year, edition, pages
Springer Nature , 2025. Vol. 16, no 1, article id 3815
National Category
Neurosciences
Identifiers
URN: urn:nbn:se:liu:diva-213255DOI: 10.1038/s41467-025-58884-2ISI: 001473866400029PubMedID: 40268901Scopus ID: 2-s2.0-105003414058OAI: oai:DiVA.org:liu-213255DiVA, id: diva2:1954564
Funder
Knut and Alice Wallenberg Foundation, NASwedish Research Council, 2022-00574Swedish Research Council, 2019-00988Swedish Research Council, 2020-01019The Swedish Brain Foundation, 2022-0219The Swedish Brain Foundation, 2022-0003The Swedish Brain Foundation, 2023-0025Swedish Heart Lung Foundation, 20210596
Note

Funding Agencies|Lions Forskningsfond mot Folksjukdomar Ph.D. support; NIH/NIGMS [R35GM131896]; Start-up funds from the Linkoeping University Wallenberg Center for Molecular Medicine / the Knut and Alice Wallenberg Foundation; Hjaernfonden (The Swedish Brain Foundation) grants [FO2022-0219, FO2022-0003, FO2023-0025]; Hjaert-Lung Fonden (The Swedish Heart-Lung Foundation) [20210596]; Vetenskapsradet (The Swedish Research Council) grants [2020-01019, 2019-00988, 2022-00574]

Available from: 2025-04-25 Created: 2025-04-25 Last updated: 2025-05-24

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Wang, KaiqianNilsson, MichelleElinder, FredrikPantazis, Antonios

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