ArticleThe journal of physiological sciences : JPS2009
CaMKII phosphorylates a threonine residue in the C-terminal tail of Cav1.2 Ca(2+) channel and modulates the interaction of the channel with calmodulin.
Article in The journal of physiological sciences : JPS, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Biological function of RNA-binding proteins in myocardial infarction: a potential emerging therapeutic limelight.Cell & bioscience · 2025Review
- Regulation of Cardiac Cav1.2 Channels by Calmodulin.International journal of molecular sciences · 2023Review
- The CaMKII phosphorylation site Thr1604 in the CaChannels (Austin, Tex.) · 2020Article
- Protein phosphorylation maintains the normal function of cloned human CaThe Journal of general physiology · 2018Article
- Inhibition of cardiac CaMKII to cure heart failure: step by step towards translation?Basic research in cardiology · 2016Article
- Abnormal alterations in the Ca²⁺/CaV1.2/calmodulin/caMKII signaling pathway in a tremor rat model and in cultured hippocampal neurons exposed to Mg²⁺-free solution.Molecular medicine reports · 2015Article
- Differential CaMKII regulation by voltage-gated calcium channels in the striatum.Molecular and cellular neurosciences · 2015Article
- Ca(2+) current facilitation is CaMKII-dependent and has arrhythmogenic consequences.Frontiers in pharmacology · 2014Review
- Mechanisms underlying the modulation of L-type Ca2+ channel by hydrogen peroxide in guinea pig ventricular myocytes.The journal of physiological sciences : JPS · 2013Article
- Nonspecific, reversible inhibition of voltage-gated calcium channels by CaMKII inhibitor CK59.Cellular and molecular neurobiology · 2013Article
- Molecular determinants for cardiovascular TRPC6 channel regulation by Ca2+/calmodulin-dependent kinase II.The Journal of physiology · 2013Article
- Facilitation of murine cardiac L-type Ca(v)1.2 channel is modulated by calmodulin kinase II-dependent phosphorylation of S1512 and S1570.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
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Abstract
We have previously found that both CaMKII-mediated phosphorylation and calmodulin (CaM) binding to the channels are required for maintaining basal activity of the Cav1.2 Ca(2+) channels. In this study, we investigated the hypothetical CaMKII phosphorylation site on Cav1.2 that contributes to the channel regulation. We found that CaMKII phosphorylates the Thr1603 residue (Thr1604 in rabbit) within the preIQ region in the C-terminal tail of the guinea-pig Cav1.2 channel. Mutation of Thr1603 to Asp (T1603D) slowed the run-down of the channel in inside-out patch mode and abolished the time-dependency of the CaM's effects to reverse run-down. We also found that CaMKII-mediated phosphorylation of the proximal C-terminal fragment (CT1) increased, while dephosphorylation of CT1 decreased its binding with CaM. These findings suggest that CaMKII regulates the CaM binding to the channel, and thereby maintains basal activity of the Cav1.2 Ca(2+) channel.
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