ArticlePflugers Archiv : European journal of physiology2008
Ca2+/CaM-dependent inactivation of the skeletal muscle L-type Ca2+ channel (Cav1.1).
Article in Pflugers Archiv : European journal of physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 34 citations in OpenAlex.
- Direct Effects of Capsaicin on Voltage-Dependent Calcium Channels of Mammalian Skeletal Muscle.Biomolecules · 2026Article
- Cytosolic peptides encoding CaCommunications biology · 2022Article
- The Crystal Structure of Calmodulin Bound to the Cardiac Ryanodine Receptor (RyR2) at Residues Phe4246-Val4271 Reveals a Fifth Calcium Binding Site.Biochemistry · 2021Article
- Calmodulin-Binding Proteins in Muscle: A Minireview on Nuclear Receptor Interacting Protein, Neurogranin, and Growth-Associated Protein 43.International journal of molecular sciences · 2020Review
- Duplex signaling by CaM and Stac3 enhances CaThe Journal of general physiology · 2018Article
- Evidence for Altered CaFrontiers in physiology · 2016Article
- Ca(2+) permeation and/or binding to CaV1.1 fine-tunes skeletal muscle Ca(2+) signaling to sustain muscle function.Skeletal muscle · 2015Article
- Towards a Unified Theory of Calmodulin Regulation (Calmodulation) of Voltage-Gated Calcium and Sodium Channels.Current molecular pharmacology · 2015Review
- Specific association of growth-associated protein 43 with calcium release units in skeletal muscles of lower vertebrates.European journal of histochemistry : EJH · 2014Article
- Calmodulin regulation (calmodulation) of voltage-gated calcium channels.The Journal of general physiology · 2014Review
- Calmodulin-dependent activation and inactivation of anoctamin calcium-gated chloride channels.The Journal of general physiology · 2013Article
- Ca(V)1.1: The atypical prototypical voltage-gated Ca²⁺ channel.Biochimica et biophysica acta · 2013Review
- Article
- Ca2+-dependent modulation of voltage-gated Ca2+ channels.Biochimica et biophysica acta · 2012Review
- Voltage clamp methods for the study of membrane currents and SR Ca(2+) release in adult skeletal muscle fibres.Progress in biophysics and molecular biology · 2012Review
- Trafficking and stability of voltage-gated calcium channels.Cellular and molecular life sciences : CMLS · 2012Review
- Alternative splicing at C terminus of Ca(V)1.4 calcium channel modulates calcium-dependent inactivation, activation potential, and current density.The Journal of biological chemistry · 2012Article
- The IQ motif is crucial for Cav1.1 function.Journal of biomedicine & biotechnology · 2011Article
- Intra- and interdomain effects due to mutation of calcium-binding sites in calmodulin.The Journal of biological chemistry · 2010Article
- Determinants in CaV1 channels that regulate the Ca2+ sensitivity of bound calmodulin.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ca2+-dependent modulation via calmodulin (CaM) has been documented for most high-voltage-activated Ca2+ channels, but whether the skeletal muscle L-type channel (Cav1.1) exhibits this property has been unknown. In this paper, whole-cell current and fluorescent resonance energy transfer (FRET) recordings were obtained from cultured mouse myotubes to test for potential involvement of CaM in function of Cav1.1. When prolonged depolarization (800 ms) was used to evoke Cav1.1 currents in normal myotubes, the fraction of current remaining at the end of the pulse displayed classic signs of Ca2+-dependent inactivation (CDI), including U-shaped voltage dependence, maximal inactivation (approximately 30%) at potentials eliciting maximal inward current, and virtual elimination of inactivation when Ba2+ replaced external Ca2+ or when 10 mM BAPTA was included in the pipette solution. Furthermore, CDI was virtually eliminated (from 30 to 8%) in normal myotubes overexpressing mutant CaM (CaM1234) that does not bind Ca2+, whereas CDI was unaltered in myotubes overexpressing wild-type CaM (CaMwt). In addition, a significant FRET signal (E=4.06%) was detected between fluorescently tagged Cav1.1 and CaMwt coexpressed in dysgenic myotubes, demonstrating for the first time that these two proteins associate in vivo. These findings show that CaM associates with and modulates Cav1.1.
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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.