ArticleChannels (Austin, Tex.)
Modulation of distinct isoforms of L-type calcium channels by G(q)-coupled receptors in Xenopus oocytes: antagonistic effects of Gβγ and protein kinase C.
Article in Channels (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Sulfolipid-1 fromJournal of neurophysiology · 2026Article
- Oxidative Regulation of Vascular CaAntioxidants (Basel, Switzerland) · 2022Review
- Reconstitution of β-adrenergic regulation of CaProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Post-Translational Modification of Cav1.2 and its Role in Neurodegenerative Diseases.Frontiers in pharmacology · 2021Review
- Regulation of cardiovascular calcium channel activity by post-translational modifications or interacting proteins.Pflugers Archiv : European journal of physiology · 2020Review
- Oxytocin Increases Phasic and Tonic GABAergic Transmission in CA1 Region of Mouse Hippocampus.Frontiers in cellular neuroscience · 2019Article
- Protein kinase C enhances plasma membrane expression of cardiac L-type calcium channel, CaChannels (Austin, Tex.) · 2017Article
- Protein kinase A regulates C-terminally truncated CaThe Journal of physiology · 2017Article
- Spexin Enhances Bowel Movement through Activating L-type Voltage-dependent Calcium Channel via Galanin Receptor 2 in Mice.Scientific reports · 2015Article
- The long and short of PKC modulation of the L-type calcium channel.Channels (Austin, Tex.)Article
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Authors and funding
6 authors at 3 institutions in 3 countries.
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No grant is acknowledged in the PubMed record.
Abstract
L-type voltage dependent Ca(2+) channels (L-VDCCs; Ca(v)1.2) are crucial in cardiovascular physiology. In heart and smooth muscle, hormones and transmitters operating via G(q) enhance L-VDCC currents via essential protein kinase C (PKC) involvement. Heterologous reconstitution studies in Xenopus oocytes suggested that PKC and G(q)-coupled receptors increased L-VDCC currents only in cardiac long N-terminus (NT) isoforms of α(1C), whereas known smooth muscle short-NT isoforms were inhibited by PKC and G(q) activators. We report a novel regulation of the long-NT α(1C) isoform by Gβγ. Gβγ inhibited whereas a Gβγ scavenger protein augmented the G(q)--but not phorbol ester-mediated enhancement of channel activity, suggesting that Gβγ acts upstream from PKC. In vitro binding experiments reveal binding of both Gβγ and PKC to α(1C)-NT. However, PKC modulation was not altered by mutations of multiple potential phosphorylation sites in the NT, and was attenuated by a mutation of C-terminally located serine S1928. The insertion of exon 9a in intracellular loop 1 rendered the short-NT α(1C) sensitive to PKC stimulation and to Gβγ scavenging. Our results suggest a complex antagonistic interplay between G(q)-activated PKC and Gβγ in regulation of L-VDCC, in which multiple cytosolic segments of α(1C) are involved.
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