ArticleBiochemistry2009
Protein kinase C isoforms differentially phosphorylate Ca(v)1.2 alpha(1c).
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 32 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
32 citing papers in PubMed, 52 citations in OpenAlex.
- Signal Override: Precision Editing of Protein Kinase Cα in Heart Failure.Circulation research · 2026Article
- Modulation of ion channels as emerging therapeutic targets in the treatment of diabetic neuropathy.EXCLI journal · 2026Review
- 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
- Increased Ca2+ influx through CaV1.2 drives aortic valve calcification.JCI insight · 2022Article
- Mechanism of adrenergic CaNature · 2020Article
- PKC and PKN in heart disease.Journal of molecular and cellular cardiology · 2019Review
- Role of Phosphatidylinositol 3-Kinase (PI3K), Mitogen-Activated Protein Kinase (MAPK), and Protein Kinase C (PKC) in Calcium Signaling Pathways Linked to the αFrontiers in physiology · 2019Article
- PKCε contributes to lipid-induced insulin resistance through cross talk with p70S6K and through previously unknown regulators of insulin signaling.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Protein Kinase C Inhibition With Ruboxistaurin Increases Contractility and Reduces Heart Size in a Swine Model of Heart Failure With Reduced Ejection Fraction.JACC. Basic to translational science · 2017Article
- Protein kinase C enhances plasma membrane expression of cardiac L-type calcium channel, CaChannels (Austin, Tex.) · 2017Article
- Prolonged ATScientific reports · 2017Article
- K(ATP) channel gain-of-function leads to increased myocardial L-type Ca(2+) current and contractility in Cantu syndrome.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- GABA(B) receptors couple to Gαq to mediate increases in voltage-dependent calcium current during development.Journal of neurochemistry · 2015Article
- Calcium-dependent PKC isoforms have specialized roles in short-term synaptic plasticity.Neuron · 2014Article
- Redox regulation of sodium and calcium handling.Antioxidants & redox signaling · 2013Review
- Ca2+ oscillations, Ca2+ sensitization, and contraction activated by protein kinase C in small airway smooth muscle.The Journal of general physiology · 2013Article
- Redox control of cardiac excitability.Antioxidants & redox signaling · 2013Review
- Hypoxic regulation of cardiac Ca2+ channel: possible role of haem oxygenase.The Journal of physiology · 2012Article
- Deletion of the C-terminal phosphorylation sites in the cardiac β-subunit does not affect the basic β-adrenergic response of the heart and the Ca(v)1.2 channel.The Journal of biological chemistry · 2012Article
Corrections and comments
- Erratum issued
Authors and funding
6 authors.
Funding
Abstract
The regulation of Ca(2+) influx through the phosphorylation of the L-type Ca(2+) channel, Ca(v)1.2, is important for the modulation of excitation-contraction (E-C) coupling in the heart. Ca(v)1.2 is thought to be the target of multiple kinases that mediate the signals of both the renin-angiotensin and sympathetic nervous systems. Detailed biochemical information regarding the protein phosphorylation reactions involved in the regulation of Ca(v)1.2 is limited. The protein kinase C (PKC) family of kinases can modulate cardiac contractility in a complex manner, such that contractility is either enhanced or depressed and relaxation is either accelerated or slowed. We have previously reported that Ser(1928) in the C-terminus of alpha(1c) was a target for PKCalpha, -zeta, and -epsilon phosphorylation. Here, we report the identification of seven PKC phosphorylation sites within the alpha(1c) subunit. Using phospho-epitope specific antibodies to Ser(1674) and Ser(1928), we demonstrate that both sites within the C-terminus are phosphorylated in HEK cells in response to PMA. Phosphorylation was inhibited with a PKC inhibitor, bisindolylmaleimide. In Langendorff-perfused rat hearts, both Ser(1674) and Ser(1928) were phosphorylated in response to PMA. Phosphorylation of Ser(1674), but not Ser(1928), is PKC isoform specific, as only PKCalpha, -betaI, -betaII, -gamma, -delta, and -theta, but not PKCepsilon, -zeta, and -eta, were able to phosphorylate this site. Our results identify a molecular mechanism by which PKC isoforms can have different effects on channel activity by phosphorylating different residues.
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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.