ArticleBiophysical journal2014
C-terminal modulatory domain controls coupling of voltage-sensing to pore opening in Cav1.3 L-type Ca(2+) channels.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- The four voltage-sensing domains of T-type calcium channels activate near the resting membrane potential.Nature communications · 2026Article
- A Novel De Novo Gain-of-FunctionNeurology. Genetics · 2024Article
- In Vitro Modulation of Spontaneous Activity in Embryonic Cardiomyocytes Cultured on Poly(vinyl alcohol)/Bioglass Type 58S Electrospun Scaffolds.Nanomaterials (Basel, Switzerland) · 2024Article
- Regulation of Cardiac Cav1.2 Channels by Calmodulin.International journal of molecular sciences · 2023Review
- Whole Exome Sequencing Identifies a Heterozygous Variant in the Cav1.3 GeneInternational journal of molecular sciences · 2022Article
- Article
- Stabilization of negative activation voltages of Cav1.3 L-Type CaChannels (Austin, Tex.) · 2021Article
- Human neuronal signaling and communication assays to assess functional neurotoxicity.Archives of toxicology · 2021Article
- Functional impact of a congenital stationary night blindness type 2 mutation depends on subunit composition of CaThe Journal of biological chemistry · 2020Article
- De novo CACNA1D CaPflugers Archiv : European journal of physiology · 2020Review
- Biophysical classification of aMolecular autism · 2020Article
- Nonlinear Input-Output Functions of Motoneurons.Physiology (Bethesda, Md.) · 2020Review
- Voltage-Gated Calcium Channels: Key Players in Sensory Coding in the Retina and the Inner Ear.Physiological reviews · 2018Review
- Gating defects of disease-causing de novo mutations in CaChannels (Austin, Tex.) · 2018Article
- Mechanisms Responsible for ω-Pore Currents in CaBiophysical journal · 2017Article
- New gain-of-function mutation shows CACNA1D as recurrently mutated gene in autism spectrum disorders and epilepsy.Human molecular genetics · 2017Article
- Lower Affinity of Isradipine for L-Type CaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2017Article
- Article
- Splice variants of the CaScientific reports · 2016Article
- Converging roles of ion channels, calcium, metabolic stress, and activity pattern of Substantia nigra dopaminergic neurons in health and Parkinson's disease.Journal of neurochemistry · 2016Review
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3 authors.
Funding
Abstract
Activity of voltage-gated Cav1.3 L-type Ca(2+) channels is required for proper hearing as well as sinoatrial node and brain function. This critically depends on their negative activation voltage range, which is further fine-tuned by alternative splicing. Shorter variants miss a C-terminal regulatory domain (CTM), which allows them to activate at even more negative potentials than C-terminally long-splice variants. It is at present unclear whether this is due to an increased voltage sensitivity of the Cav1.3 voltage-sensing domain, or an enhanced coupling of voltage-sensor conformational changes to the subsequent opening of the activation gate. We studied the voltage-dependence of voltage-sensor charge movement (QON-V) and of current activation (ICa-V) of the long (Cav1.3L) and a short Cav1.3 splice variant (Cav1.342A) expressed in tsA-201 cells using whole cell patch-clamp. Charge movement (QON) of Cav1.3L displayed a much steeper voltage-dependence and a more negative half-maximal activation voltage than Cav1.2 and Cav3.1. However, a significantly higher fraction of the total charge had to move for activation of Cav1.3 half-maximal conductance (Cav1.3: 68%; Cav1.2: 52%; Cav3.1: 22%). This indicated a weaker coupling of Cav1.3 voltage-sensor charge movement to pore opening. However, the coupling efficiency was strengthened in the absence of the CTM in Cav1.342A, thereby shifting ICa-V by 7.2 mV to potentials that were more negative without changing QON-V. We independently show that the presence of intracellular organic cations (such as n-methyl-D-glucamine) induces a pronounced negative shift of QON-V and a more negative activation of ICa-V of all three channels. These findings illustrate that the voltage sensors of Cav1.3 channels respond more sensitively to depolarization than those of Cav1.2 or Cav3.1. Weak coupling of voltage sensing to pore opening is enhanced in the absence of the CTM, allowing short Cav1.342A splice variants to activate at lower voltages without affecting QON-V.
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