ArticleBiophysical journal2008
Alpha2delta1 dihydropyridine receptor subunit is a critical element for excitation-coupled calcium entry but not for formation of tetrads in skeletal myotubes.
Article in Biophysical journal, 2008. 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.
- ERG1A KScientific reports · 2025Article
- Disruption of the Key CaCell reports · 2019Article
- Interactions of Dichlorodiphenyltrichloroethane (DDT) and Dichlorodiphenyldichloroethylene (DDE) With Skeletal Muscle Ryanodine Receptor Type 1.Toxicological sciences : an official journal of the Society of Toxicology · 2019Article
- Junctional trafficking and restoration of retrograde signaling by the cytoplasmic RyR1 domain.The Journal of general physiology · 2018Article
- De novo reconstitution reveals the proteins required for skeletal muscle voltage-induced CaProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Functional impact of an oculopharyngeal muscular dystrophy mutation in PABPN1.The Journal of physiology · 2017Article
- Stac3 has a direct role in skeletal muscle-type excitation-contraction coupling that is disrupted by a myopathy-causing mutation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Mechanisms of the gabapentinoids and α 2 δ-1 calcium channel subunit in neuropathic pain.Pharmacology research & perspectives · 2016Review
- The Physiology, Pathology, and Pharmacology of Voltage-Gated Calcium Channels and Their Future Therapeutic Potential.Pharmacological reviews · 2015Review
- 3D Structure of the Dihydropyridine Receptor of Skeletal Muscle.European journal of translational myology · 2015Review
- Amino acid residues 489-503 of dihydropyridine receptor (DHPR) β1a subunit are critical for structural communication between the skeletal muscle DHPR complex and type 1 ryanodine receptor.The Journal of biological chemistry · 2014Article
- β1a490-508, a 19-residue peptide from C-terminal tail of Cav1.1 β1a subunit, potentiates voltage-dependent calcium release in adult skeletal muscle fibers.Biophysical journal · 2014Article
- Ca(V)1.1: The atypical prototypical voltage-gated Ca²⁺ channel.Biochimica et biophysica acta · 2013Review
- Calcium channel auxiliary α2δ and β subunits: trafficking and one step beyond.Nature reviews. Neuroscience · 2012Review
- Trafficking and stability of voltage-gated calcium channels.Cellular and molecular life sciences : CMLS · 2012Review
- Divergent biophysical properties, gating mechanisms, and possible functions of the two skeletal muscle Ca(V)1.1 calcium channel splice variants.Journal of muscle research and cell motility · 2011Article
- Reciprocal dihydropyridine and ryanodine receptor interactions in skeletal muscle activation.Journal of muscle research and cell motility · 2011Review
- Two inhibitors of store operated Ca2+ entry suppress excitation contraction coupling in frog skeletal muscle.Journal of muscle research and cell motility · 2010Article
- Smooth muscle cell alpha2delta-1 subunits are essential for vasoregulation by CaV1.2 channels.Circulation research · 2009Article
- Checking your SOCCs and feet: the molecular mechanisms of Ca2+ entry in skeletal muscle.The Journal of physiology · 2009Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
It has been shown that small interfering RNA (siRNA) partial knockdown of the alpha(2)delta(1) dihydropyridine receptor subunits cause a significant increase in the rate of activation of the L-type Ca(2+) current in myotubes but have little or no effect on skeletal excitation-contraction coupling. This study used permanent siRNA knockdown of alpha(2)delta(1) to address two important unaddressed questions. First, does the alpha(2)delta(1) subunit contribute to the size and/or spacing of tetradic particles? Second, is the alpha(2)delta(1) subunit important for excitation-coupled calcium entry? We found that the size and spacing of tetradic particles is unaffected by siRNA knockdown of alpha(2)delta(1), indicating that the visible particle represents the alpha(1s) subunit. Strikingly, >97% knockdown of alpha(2)delta(1) leads to a complete loss of excitation-coupled calcium entry during KCl depolarization and a more rapid decay of Ca(2+) transients during bouts of repetitive electrical stimulation like those occurring during normal muscle activation in vivo. Thus, we conclude that the alpha(2)delta(1) dihydropyridine receptor subunit is physiologically necessary for sustaining Ca(2+) transients in response to prolonged depolarization or repeated trains of action potentials.
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