ArticleThe Journal of physiology2005
Arachidonate-regulated Ca2+-selective (ARC) channel activity is modulated by phosphorylation and involves an A-kinase anchoring protein.
Article in The Journal of physiology, 2005. 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed.
- p38 MAPK activation and STIM1-Orai3 association mediate TRPC6 externalization.American journal of physiology. Cell physiology · 2023Article
- Functional communication between IPProceedings of the National Academy of Sciences of the United States of America · 2022Article
- CREB regulates the expression of type 1 inositol 1,4,5-trisphosphate receptors.Journal of cell science · 2021Article
- Selective activation of distinct Orai channels by STIM1.Cell calcium · 2017Review
- Anchoring protein AKAP79-mediated PKA phosphorylation of STIM1 determines selective activation of the ARC channel, a store-independent Orai channel.The Journal of physiology · 2015Article
- Arachidonate-regulated Ca(2+) influx in human airway smooth muscle.American journal of respiratory cell and molecular biology · 2014Article
- Acid-sensing ion channels in pathological conditions.Advances in experimental medicine and biology · 2013Review
- Modulation of acid-sensing ion channels: molecular mechanisms and therapeutic potential.International journal of physiology, pathophysiology and pharmacology · 2011Article
- Arachidonic acid, ARC channels, and Orai proteins.Cell calcium · 2009Review
- Inhibition of serine/threonine phosphatase enhances arachidonic acid-induced [Ca2+]i via protein kinase A.American journal of physiology. Cell physiology · 2009Article
- Agonist-induced calcium entry correlates with STIM1 translocation.Journal of cellular physiology · 2007Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
In many non-excitable cells, the predominant mode of agonist-activated Ca(2+) entry switches from the arachidonic acid-regulated Ca(2+) (ARC) channels at low agonist concentrations, to store-operated channels at high concentrations. Underlying this process is the inhibition of the ARC channels by a calcineurin-mediated dephosphorylation, which inhibits the ability of arachidonic acid to activate the channels. Following such a dephosphorylation, we found that restoration of the sensitivity of the ARC channels to arachidonic acid, as well as to low concentrations of carbachol, was specifically dependent on protein kinase A (PKA) activity. Inhibition of protein kinase C, protein kinase G or calmodulin-activated kinase had no effect. This action of PKA was unaffected by prolonged intracellular dialysis, whilst disruption of the binding of PKA to A-kinase anchoring proteins (AKAPs) inhibited currents through ARC channels, and blocked the PKA-dependent effects. AKAP79, a protein which scaffolds both PKA and calcineurin, was shown to be present in the cells. These data illustrate the significance of PKA-dependent phosphorylation and calcineurin-dependent dephosphorylation in the overall regulation of ARC channel activity, and indicate the key role of an AKAP, possibly AKAP79, in the spatial organization these processes.
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Registered trials
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