ArticleThe Journal of biological chemistry2010
Molecular determinants of the CaVbeta-induced plasma membrane targeting of the CaV1.2 channel.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 33 citations in OpenAlex.
- Clustering of CaJournal of neurochemistry · 2023Article
- Regulation of Cardiac Cav1.2 Channels by Calmodulin.International journal of molecular sciences · 2023Review
- Sympathetic Stimulation Upregulates the CaCells · 2022Article
- The life cycle of voltage-gated CaNeuronal signaling · 2021Review
- α-Actinin-1 promotes activity of the L-type CaThe EMBO journal · 2020Article
- An African loss-of-function CACNA1C variant p.T1787M associated with a risk of ventricular fibrillation.Scientific reports · 2018Article
- Negatively charged residues in the first extracellular loop of the L-type CaThe Journal of biological chemistry · 2017Article
- α-Actinin Promotes Surface Localization and Current Density of the CaBiochemistry · 2017Article
- Proteolytic cleavage of the hydrophobic domain in the CaThe Journal of biological chemistry · 2017Article
- Stapled Voltage-Gated Calcium Channel (CaACS chemical neuroscience · 2017Article
- Trafficking of neuronal calcium channels.Neuronal signaling · 2017Review
- Determination of the Relative Cell Surface and Total Expression of Recombinant Ion Channels Using Flow Cytometry.Journal of visualized experiments : JoVE · 2016Article
- Identification of Glycosylation Sites Essential for Surface Expression of the CaVα2δ1 Subunit and Modulation of the Cardiac CaV1.2 Channel Activity.The Journal of biological chemistry · 2016Article
- Direct interaction of CaVβ with actin up-regulates L-type calcium currents in HL-1 cardiomyocytes.The Journal of biological chemistry · 2015Article
- Functional characterization of CaVα2δ mutations associated with sudden cardiac death.The Journal of biological chemistry · 2015Article
- Potentiation of high voltage-activated calcium channels by 4-aminopyridine depends on subunit composition.Molecular pharmacology · 2014Article
- Cooperative activation of the T-type CaV3.2 channel: interaction between Domains II and III.The Journal of biological chemistry · 2013Article
- A quartet of leucine residues in the guanylate kinase domain of CaVβ determines the plasma membrane density of the CaV2.3 channel.The Journal of biological chemistry · 2012Article
- Trafficking and stability of voltage-gated calcium channels.Cellular and molecular life sciences : CMLS · 2012Review
- Mechanism of auxiliary β-subunit-mediated membrane targeting of L-type (Ca(V)1.2) channels.The Journal of physiology · 2011Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Ca(V)beta subunits modulate cell surface expression and voltage-dependent gating of high voltage-activated (HVA) Ca(V)1 and Ca(V)2 alpha1 subunits. High affinity Ca(V)beta binding onto the so-called alpha interaction domain of the I-II linker of the Ca(V)alpha1 subunit is required for Ca(V)beta modulation of HVA channel gating. It has been suggested, however, that Ca(V)beta-mediated plasma membrane targeting could be uncoupled from Ca(V)beta-mediated modulation of channel gating. In addition to Ca(V)beta, Ca(V)alpha2delta and calmodulin have been proposed to play important roles in HVA channel targeting. Indeed we show that co-expression of Ca(V)alpha2delta caused a 5-fold stimulation of the whole cell currents measured with Ca(V)1.2 and Ca(V)beta3. To gauge the synergetic role of auxiliary subunits in the steady-state plasma membrane expression of Ca(V)1.2, extracellularly tagged Ca(V)1.2 proteins were quantified using fluorescence-activated cell sorting analysis. Co-expression of Ca(V)1.2 with either Ca(V)alpha2delta, calmodulin wild type, or apocalmodulin (alone or in combination) failed to promote the detection of fluorescently labeled Ca(V)1.2 subunits. In contrast, co-expression with Ca(V)beta3 stimulated plasma membrane expression of Ca(V)1.2 by a 10-fold factor. Mutations within the alpha interaction domain of Ca(V)1.2 or within the nucleotide kinase domain of Ca(V)beta3 disrupted the Ca(V)beta3-induced plasma membrane targeting of Ca(V)1.2. Altogether, these data support a model where high affinity binding of Ca(V)beta to the I-II linker of Ca(V)alpha1 largely accounts for Ca(V)beta-induced plasma membrane targeting of Ca(V)1.2.
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