ArticleMolecular and cellular biochemistry1998
cAMP-dependent phosphorylation sites and macroscopic activity of recombinant cardiac L-type calcium channels.
Article in Molecular and cellular biochemistry, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- The psychiatric risk gene CACNA1C encodes distinct full-length isoforms in human brain, heart and aorta.Molecular psychiatry · 2026Article
- Cell-cell communication: new insights and clinical implications.Signal transduction and targeted therapy · 2024Review
- The quest to identify the mechanism underlying adrenergic regulation of cardiac CaChannels (Austin, Tex.) · 2020Review
- CaV1.2 signaling complexes in the heart.Journal of molecular and cellular cardiology · 2013Review
- Oestrogen upregulates L-type Ca²⁺ channels via oestrogen-receptor- by a regional genomic mechanism in female rabbit hearts.The Journal of physiology · 2012Article
- Supramolecular assemblies and localized regulation of voltage-gated ion channels.Physiological reviews · 2009Review
- Beta-adrenergic stimulation of L-type Ca2+ channels in cardiac myocytes requires the distal carboxyl terminus of alpha1C but not serine 1928.Circulation research · 2006Article
- The L-type calcium channel in the heart: the beat goes on.The Journal of clinical investigation · 2005Review
- Direct and remote modulation of L-channels in chromaffin cells: distinct actions on alpha1C and alpha1D subunits?Molecular neurobiology · 2004Review
- Regulation of L-type Ca2+ channels in the heart: overview of recent advances.Molecular and cellular biochemistry · 2003Review
- Characterization of auto-regulation of the human cardiac alpha1 subunit of the L-type calcium channel: importance of the C-terminus.Molecular and cellular biochemistry · 2003Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
The involvement of cAMP-dependent phosphorylation sites in establishing the basal activity of cardiac L-type Ca2+ channels was studied in HEK 293 cells transiently cotransfected with mutants of the human cardiac alpha1 and accessory subunits. Systematic individual or combined elimination of high consensus protein kinase A (PKA) sites, by serine to alanine substitutions at the amino and carboxyl termini of the alpha1 subunit, resulted in Ca2+ channel currents indistinguishable from those of wild type channels. Dihydropyridine (DHP)-binding characteristics were also unaltered. To explore the possible involvement of nonconsensus sites, deletion mutants were used. Carboxyl-terminal truncations of the alpha1 subunit distal to residue 1597 resulted in increased channel expression and current amplitudes. Modulation of PKA activity in cells transfected with the wild type channel or any of the mutants did not alter Ca2+ channel functions suggesting that cardiac Ca2+ channels expressed in these cells behave, in terms of lack of PKA control, like Ca2+ channels of smooth muscle cells.
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Registered trials
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.