ArticleProceedings of the National Academy of Sciences of the United States of America2010
Beta-adrenergic-regulated phosphorylation of the skeletal muscle Ca(V)1.1 channel in the fight-or-flight response.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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
33 citing papers in PubMed, 60 citations in OpenAlex.
- BetaThe Journal of physiology · 2018Trial
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- Single-chain fluorescent integrators for mapping G-protein-coupled receptor agonists.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
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- Transcriptomic, proteomic and phosphoproteomic underpinnings of daily exercise performance and zeitgeber activity of training in mouse muscle.The Journal of physiology · 2022Article
- Exploring the Muscle Metabolomics in the Mouse Model of Sepsis-Induced Acquired Weakness.Evidence-based complementary and alternative medicine : eCAM · 2022Article
- The quest to identify the mechanism underlying adrenergic regulation of cardiac CaChannels (Austin, Tex.) · 2020Review
- Unraveling the mechanobiology of immune cells.Current opinion in biotechnology · 2020Review
- Pedal serotonergic neuron clusters of the pteropod mollusc, Clione limacina, contain two morphological subtypes with different innervation targets.Invertebrate neuroscience : IN · 2020Article
- Effects of adrenaline on contractility and endurance of isolated mammalian soleus with different calcium concentrations.Journal of muscle research and cell motility · 2019Article
- Regulation of microdomain voltage-gated L-type calcium channels in cardiac health and disease.Current opinion in physiology · 2018Article
- Identification of a novel cAMP dependent protein kinase A phosphorylation site on the human cardiac calcium channel.Scientific reports · 2017Article
- Loss of β-adrenergic-stimulated phosphorylation of CaV1.2 channels on Ser1700 leads to heart failure.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- 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
- Phosphorylation of the Cav3.2 T-type calcium channel directly regulates its gating properties.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- β-Adrenergic modulation of skeletal muscle contraction: key role of excitation-contraction coupling.The Journal of physiology · 2015Review
- Phosphorylation sites in the Hook domain of CaVβ subunits differentially modulate CaV1.2 channel function.Journal of molecular and cellular cardiology · 2015Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Ca(V)1 channels initiate excitation-contraction coupling in skeletal and cardiac muscle. During the fight-or-flight response, epinephrine released by the adrenal medulla and norepinephrine released from sympathetic nerves increase muscle contractility by activation of the β-adrenergic receptor/cAMP-dependent protein kinase pathway and up-regulation of Ca(V)1 channels in skeletal and cardiac muscle. Although the physiological mechanism of this pathway is well defined, the molecular mechanism and the sites of protein phosphorylation required for Ca(V)1 channel regulation are unknown. To identify the regulatory sites of phosphorylation under physiologically relevant conditions, Ca(V)1.1 channels were purified from skeletal muscle and sites of phosphorylation on the α1 subunit were identified by mass spectrometry. Two phosphorylation sites were identified in the proximal C-terminal domain, serine 1575 (S1575) and threonine 1579 (T1579), which are conserved in cardiac Ca(V)1.2 channels (S1700 and T1704, respectively). In vitro phosphorylation revealed that Ca(V)1.1-S1575 is a substrate for both cAMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase II, whereas Ca(V)1.1-T1579 is a substrate for casein kinase 2. Treatment of rabbits with isoproterenol to activate β-adrenergic receptors increased phosphorylation of S1575 in skeletal muscle Ca(V)1.1 channels in vivo, and treatment with propranolol to inhibit β-adrenergic receptors reduced phosphorylation. As S1575 and T1579 in Ca(V)1.1 channels and their homologs in Ca(V)1.2 channels are located at a key regulatory interface between the distal and proximal C-terminal domains, it is likely that phosphorylation of these sites in skeletal and cardiac muscle is directly involved in calcium channel regulation in response to the sympathetic nervous system in the fight-or-flight response.
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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.