ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2011
Cardiac L-type calcium channel (Cav1.2) associates with gamma subunits.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed.
- Local calcium dynamics and signalling in cardiomyocytes.Nature reviews. Cardiology · 2026Review
- Electrophysiological Mechanisms and Therapeutic Potential of Calcium Channels in Atrial Fibrillation.Reviews in cardiovascular medicine · 2025Review
- A membrane-associated phosphoswitch in Rad controls adrenergic regulation of cardiac calcium channels.The Journal of clinical investigation · 2024Article
- Rad regulation of CaNature cardiovascular research · 2022Article
- Harm of circadian misalignment to the hearts of the adolescent wistar rats.Journal of translational medicine · 2022Article
- Mechanisms and physiological implications of cooperative gating of clustered ion channels.Physiological reviews · 2022Review
- The Calcium Channel Subunit Gamma-4 as a Novel Regulator of MafA in Pancreatic Beta-Cell Controls Glucose Homeostasis.Biomedicines · 2022Article
- Increased Ca2+ influx through CaV1.2 drives aortic valve calcification.JCI insight · 2022Article
- Deciphering the Interactions of SARS-CoV-2 Proteins with Human Ion Channels Using Machine-Learning-Based Methods.Pathogens (Basel, Switzerland) · 2022Article
- Cerebrospinal fluid proteomics targeted for central nervous system processes in bipolar disorder.Molecular psychiatry · 2021Article
- Role of High Voltage-Gated CaCells · 2021Review
- Mechanisms and Regulation of Cardiac CaInternational journal of molecular sciences · 2021Review
- Regulation of cardiovascular calcium channel activity by post-translational modifications or interacting proteins.Pflugers Archiv : European journal of physiology · 2020Review
- Mechanism of adrenergic CaNature · 2020Article
- Article
- Dysfunctional Cav1.2 channel in Timothy syndrome, from cell to bedside.Experimental biology and medicine (Maywood, N.J.) · 2019Article
- Atomic Mechanisms of Timothy Syndrome-Associated Mutations in Calcium Channel Cav1.2.Frontiers in physiology · 2019Article
- The calcium channel subunit gamma-4 is regulated by MafA and necessary for pancreatic beta-cell specification.Communications biology · 2019Article
- Mutations in voltage-gated L-type calcium channel: implications in cardiac arrhythmia.Channels (Austin, Tex.) · 2018Review
- The Pattern of mRNA Expression Is Changed in Sinoatrial Node from Goto-Kakizaki Type 2 Diabetic Rat Heart.Journal of diabetes research · 2018Article
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5 authors.
Funding
Abstract
The cardiac voltage-gated Ca(2+) channel, Ca(v)1.2, mediates excitation-contraction coupling in the heart. The molecular composition of the channel includes the pore-forming α1 subunit and auxiliary α2/δ-1 and β subunits. Ca(2+) channel γ subunits, of which there are 8 isoforms, consist of 4 transmembrane domains with intracellular N- and C-terminal ends. The γ1 subunit was initially detected in the skeletal muscle Ca(v)1.1 channel complex, modulating current amplitude and activation and inactivation properties. The γ1 subunit also shifts the steady-state inactivation to more negative membrane potentials, accelerates current inactivation, and increases peak currents, when coexpressed with the cardiac α1c subunit in Xenopus oocytes and human embryonic kidney (HEK) 293 cells. The γ1 subunit is not expressed, however, in cardiac muscle. We sought to determine whether γ subunits that are expressed in cardiac tissue physically associate with and modulate Ca(v)1.2 function. We now demonstrate that γ4, γ6, γ7, and γ8 subunits physically interact with the Ca(v)1.2 complex. The γ subunits differentially modulate Ca(2+) channel function when coexpressed with the β1b and α2/δ-1 subunits in HEK cells, altering both activation and inactivation properties. The effects of γ on Ca(v)1.2 function are dependent on the subtype of β subunit. Our results identify new members of the cardiac Ca(v)1.2 macromolecular complex and identify a mechanism by which to increase the functional diversity of Ca(v)1.2 channels.
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