{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1360002218651397760.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1152/ajpcell.00267.2014"}},{"identifier":{"@type":"URI","@value":"https://journals.physiology.org/doi/pdf/10.1152/ajpcell.00267.2014"}},{"identifier":{"@type":"PMID","@value":"25209265"}}],"resourceType":"学術雑誌論文(journal article)","dc:title":[{"@value":"A new phosphorylation site in cardiac L-type Ca<sup>2+</sup> channels (Cav1.2) responsible for its cAMP-mediated modulation"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p> Cardiac L-type Ca<jats:sup>2+</jats:sup> channels are modulated by phosphorylation by protein kinase A (PKA). To explore the PKA-targeted phosphorylation site(s), five potential phosphorylation sites in the carboxyl (COOH) terminal region of the α<jats:sub>1C</jats:sub>-subunit of the guinea pig Cav1.2 Ca<jats:sup>2+</jats:sup> channel were mutated by replacing serine (S) or threonine (T) residues with alanine (A): S1574A (C1 site), S1626A (C2), S1699A (C3), T1908A, (C4), S1927A (C5), and their various combinations. The wild-type Ca<jats:sup>2+</jats:sup> channel activity was enhanced three- to fourfold by the adenylyl cyclase activator forskolin (Fsk, 5 μM), and that of mutants at C3, C4, C5, and combination of these sites was also significantly increased by Fsk. However, Fsk did not modulate the activity of the C1 and C2 mutants and mutants of combined sites involving the C1 site. Three peptides of the COOH-terminal tail of α<jats:sub>1C</jats:sub>, termed CT1 [corresponding to amino acids (aa) 1509–1789, containing sites C1–3], CT2 (aa 1778–2003, containing sites C4 and C5), and CT3 (aa 1942–2169), were constructed, and their phosphorylation by PKA was examined. CT1 and CT2, but not CT3, were phosphorylated in vitro by PKA. Three CT1 mutants at two sites of C1-C3 were also phosphorylated by PKA, but the mutant at all three sites was not. The CT2 mutant at the C4 site was phosphorylated by PKA, but the mutant at C5 sites was not. These results suggest that Ser<jats:sup>1574</jats:sup> (C1 site) may be a potential site for the channel modulation mediated by PKA. </jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1420001326216190080","@type":"Researcher","personIdentifier":[{"@type":"KAKEN_RESEARCHERS","@value":"00448581"},{"@type":"NRID","@value":"1000000448581"},{"@type":"NRID","@value":"9000002184185"},{"@type":"NRID","@value":"9000020132545"},{"@type":"NRID","@value":"9000392138141"},{"@type":"NRID","@value":"9000257908151"},{"@type":"NRID","@value":"9000107314598"},{"@type":"NRID","@value":"9000020127227"},{"@type":"NRID","@value":"9000272990863"},{"@type":"RESEARCHMAP","@value":"https://researchmap.jp/221-mimiben"}],"foaf:name":[{"@value":"Etsuko Minobe"}],"jpcoar:affiliationName":[{"@value":"Department of Physiology, Graduate School of Medical & Dental Sciences, Kagoshima University, Kagoshima, Japan;"}]},{"@id":"https://cir.nii.ac.jp/crid/1380566396878184193","@type":"Researcher","foaf:name":[{"@value":"Sachiko Maeda"}],"jpcoar:affiliationName":[{"@value":"Department of Physiology, Graduate School of Medical & Dental Sciences, Kagoshima University, Kagoshima, Japan;"},{"@value":"Department of Cellular Physiology and Signal Transduction, Sapporo Medical University School of Medicine, Sapporo, Japan; and"}]},{"@id":"https://cir.nii.ac.jp/crid/1380566396878184322","@type":"Researcher","foaf:name":[{"@value":"Liying Hao"}],"jpcoar:affiliationName":[{"@value":"Department of Physiology, Graduate School of Medical & Dental Sciences, Kagoshima University, Kagoshima, Japan;"},{"@value":"Department of Pharmaceutical Toxicology, School of Pharmaceutical Sciences, China Medical University, Shenyang, China"}]},{"@id":"https://cir.nii.ac.jp/crid/1420001326206372480","@type":"Researcher","personIdentifier":[{"@type":"KAKEN_RESEARCHERS","@value":"10581689"},{"@type":"NRID","@value":"1000010581689"},{"@type":"NRID","@value":"9000272990864"},{"@type":"RESEARCHMAP","@value":"https://researchmap.jp/xu-86"}],"foaf:name":[{"@value":"Jianjun Xu"}],"jpcoar:affiliationName":[{"@value":"Department of Physiology, Graduate School of Medical & Dental Sciences, Kagoshima University, Kagoshima, Japan;"}]},{"@id":"https://cir.nii.ac.jp/crid/1380566396878184323","@type":"Researcher","foaf:name":[{"@value":"Asako Kameyama"}],"jpcoar:affiliationName":[{"@value":"Department of Physiology, Graduate School of Medical & Dental Sciences, Kagoshima University, Kagoshima, Japan;"}]},{"@id":"https://cir.nii.ac.jp/crid/1380566396878184192","@type":"Researcher","foaf:name":[{"@value":"Masaki Kameyama"}],"jpcoar:affiliationName":[{"@value":"Department of Physiology, Graduate School of Medical & Dental Sciences, Kagoshima University, Kagoshima, Japan;"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"03636143"},{"@type":"EISSN","@value":"15221563"}],"prism:publicationName":[{"@value":"American Journal of Physiology-Cell Physiology"}],"dc:publisher":[{"@value":"American Physiological Society"}],"prism:publicationDate":"2014-12-01","prism:volume":"307","prism:number":"11","prism:startingPage":"C999","prism:endingPage":"C1009"},"reviewed":"false","url":[{"@id":"https://journals.physiology.org/doi/pdf/10.1152/ajpcell.00267.2014"}],"createdAt":"2014-09-11","modifiedAt":"2024-06-17","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=Amino%20Acid%20Transport%20System%20ASC","dc:title":"Amino Acid Transport System ASC"},{"@id":"https://cir.nii.ac.jp/all?q=Calcium%20Channels,%20L-Type","dc:title":"Calcium Channels, L-Type"},{"@id":"https://cir.nii.ac.jp/all?q=Epithelial%20Cells","dc:title":"Epithelial Cells"},{"@id":"https://cir.nii.ac.jp/all?q=Phosphatidylethanolamine%20Binding%20Protein","dc:title":"Phosphatidylethanolamine Binding Protein"},{"@id":"https://cir.nii.ac.jp/all?q=Cell%20Line","dc:title":"Cell Line"},{"@id":"https://cir.nii.ac.jp/all?q=Leukotriene%20D4","dc:title":"Leukotriene D4"},{"@id":"https://cir.nii.ac.jp/all?q=Rats","dc:title":"Rats"},{"@id":"https://cir.nii.ac.jp/all?q=Proto-Oncogene%20Proteins%20c-raf","dc:title":"Proto-Oncogene Proteins c-raf"},{"@id":"https://cir.nii.ac.jp/all?q=Gene%20Expression%20Regulation","dc:title":"Gene Expression Regulation"},{"@id":"https://cir.nii.ac.jp/all?q=Catalytic%20Domain","dc:title":"Catalytic Domain"},{"@id":"https://cir.nii.ac.jp/all?q=Cyclic%20AMP","dc:title":"Cyclic AMP"},{"@id":"https://cir.nii.ac.jp/all?q=Animals","dc:title":"Animals"},{"@id":"https://cir.nii.ac.jp/all?q=Intestinal%20Mucosa","dc:title":"Intestinal Mucosa"},{"@id":"https://cir.nii.ac.jp/all?q=Phosphorylation","dc:title":"Phosphorylation"}],"project":[{"@id":"https://cir.nii.ac.jp/crid/1040282257234704768","@type":"Project","projectIdentifier":[{"@type":"KAKEN","@value":"25460294"},{"@type":"JGN","@value":"JP25460294"},{"@type":"URI","@value":"https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-25460294/"}],"notation":[{"@language":"ja","@value":"カルモジュリンによるL型Caチャネルの活性制御の分子機構の解明"},{"@language":"en","@value":"Ca2+ and calmodulin-dependent inactivation of the L-type Ca2+ channel and its mutants"}]}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360004236318603904","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"PKA and phosphatases attached to the Ca<sub>V</sub>1.2 channel regulate channel activity in cell-free 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cardiac L-type Ca current suggest two sites are phosphorylated by protein kinase A and another protein kinase."}]},{"@id":"https://cir.nii.ac.jp/crid/1361418521139596416","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Ser<sup>1901</sup> of α<sub>1C</sub> subunit is required for the PKA‐mediated enhancement of L‐type Ca<sup>2+</sup> channel currents but not for the negative shift of activation"}]},{"@id":"https://cir.nii.ac.jp/crid/1361699994991852672","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"A potential site of functional modulation by protein kinase A in the cardiac Ca<sup>2+</sup> channel <i>α</i><sub>1C</sub> subunit"}]},{"@id":"https://cir.nii.ac.jp/crid/1361699995053325568","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Regulation of Cardiac L-Type Ca\n            <sup>2+</sup>\n            Channel Ca\n            <sub>V</sub>\n            1.2 Via the β-Adrenergic-cAMP-Protein Kinase A Pathway"}]},{"@id":"https://cir.nii.ac.jp/crid/1361981470832917376","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Deletion of the Distal C Terminus of CaV1.2 Channels Leads to Loss of β-Adrenergic Regulation and Heart Failure in Vivo"}]},{"@id":"https://cir.nii.ac.jp/crid/1362262943976636672","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Calmodulin Is the Ca2+ Sensor for Ca2+-Dependent Inactivation of L-Type Calcium Channels"}]},{"@id":"https://cir.nii.ac.jp/crid/1362262945288523520","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"β‐Adrenergic stimulation modulates Ca<sup>2+</sup>‐ and voltage‐dependent inactivation of L‐type Ca<sup>2+</sup> channel currents in guinea‐pig ventricular myocytes"}]},{"@id":"https://cir.nii.ac.jp/crid/1362544418367774976","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Identification of the Sites Phosphorylated by Cyclic AMP-Dependent Protein Kinase on the β<sub>2</sub> Subunit of L-Type Voltage-Dependent Calcium Channels<sup>†</sup>"}]},{"@id":"https://cir.nii.ac.jp/crid/1362544418632998528","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Voltage-dependent potentiation of the activity of cardiac L-type calcium channel alpha 1 subunits due to phosphorylation by cAMP-dependent protein kinase."}]},{"@id":"https://cir.nii.ac.jp/crid/1362544418909892480","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Molecular Mechanism of Calcium Channel Regulation in the Fight-or-Flight Response"}]},{"@id":"https://cir.nii.ac.jp/crid/1362544419033334144","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Deletion of the C-terminal Phosphorylation Sites in the Cardiac β-Subunit Does Not Affect the Basic β-Adrenergic Response of the Heart and the Cav1.2 Channel"}]},{"@id":"https://cir.nii.ac.jp/crid/1362544421384325888","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"β-Adrenergic regulation requires direct anchoring of PKA to cardiac Ca\n            <sub>V</sub>\n            1.2 channels via a leucine zipper interaction with A kinase-anchoring protein 15"}]},{"@id":"https://cir.nii.ac.jp/crid/1362825894122016640","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Two distinct inactivation processes related to phosphorylation in cardiac L-type Ca<sup>2+</sup> channel currents"}]},{"@id":"https://cir.nii.ac.jp/crid/1362825894280236672","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Regulation and modulation of calcium channels in cardiac, skeletal, and smooth muscle cells"}]},{"@id":"https://cir.nii.ac.jp/crid/1362825894918301312","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Regulation of Cardiac L-Type Calcium Channels by Protein Kinase A and Protein Kinase C"}]},{"@id":"https://cir.nii.ac.jp/crid/1362825896152358528","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Phosphorylation sites required for regulation of cardiac calcium channels in the fight-or-flight response"}]},{"@id":"https://cir.nii.ac.jp/crid/1363107370185787520","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Supramolecular Assemblies and Localized Regulation of Voltage-Gated Ion Channels"}]},{"@id":"https://cir.nii.ac.jp/crid/1363388844665875328","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"cAMP-dependent phosphorylation of the cardiac L-type Ca channel: A missing link?"}]},{"@id":"https://cir.nii.ac.jp/crid/1363388845975822080","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Regulation of the cloned L‐type cardiac calcium channel by cyclic‐AMP‐dependent protein kinase"}]},{"@id":"https://cir.nii.ac.jp/crid/1363388846203136768","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"?-Subunit expression is required for cAMP-dependent increase of cloned cardiac and vascular calcium channel currents"}]},{"@id":"https://cir.nii.ac.jp/crid/1363670318337177344","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"cAMP-Dependent Regulation of Cardiac L-Type Ca2+ Channels Requires Membrane Targeting of PKA and Phosphorylation of Channel Subunits"}]},{"@id":"https://cir.nii.ac.jp/crid/1363670320160539264","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Molecular aspects of adrenergic modulation of cardiac L-type Ca channels"}]},{"@id":"https://cir.nii.ac.jp/crid/1363670320701783552","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Cyclic AMP-vepenvent protein kinase phosphorylates residues in the C-terminal domain of the cardiac L-type calcium channel α1 subunit"}]},{"@id":"https://cir.nii.ac.jp/crid/1363951793515350144","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Cyclic AMP‐dependent phosphorylation and regulation of the cardiac dihydropyridine‐sensitive Ca channel"}]},{"@id":"https://cir.nii.ac.jp/crid/1363951794815884416","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Specific Phosphorylation of a Site in the Full-Length Form of the α1 Subunit of the Cardiac L-Type Calcium Channel by Adenosine 3‘,5‘-Cyclic Monophosphate- Dependent Protein Kinase"}]},{"@id":"https://cir.nii.ac.jp/crid/1363951795959796608","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"β-Adrenergic modulation of calcium channels in frog ventricular heart cells"}]},{"@id":"https://cir.nii.ac.jp/crid/1364233268574994816","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Opposite effects of phosphatase inhibitors on L‐type calcium and delayed rectifier currents in frog cardiac myocytes."}]},{"@id":"https://cir.nii.ac.jp/crid/1364233268917472896","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Differential regulation of CaV1.2 channels by cAMP-dependent protein kinase bound to A-kinase anchoring proteins 15 and 79/150"}]},{"@id":"https://cir.nii.ac.jp/crid/1364233268976324480","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Cloning and Expression of the Ca2+ Channel  1c and  2a Subunits from Guinea Pig Heart"}]},{"@id":"https://cir.nii.ac.jp/crid/1364233270120493952","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Cardiomyocytes from AKAP7 knockout mice respond normally to adrenergic stimulation"}]},{"@id":"https://cir.nii.ac.jp/crid/1364233270307031424","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"β-Adrenergic Stimulation of L-type Ca\n                    <sup>2+</sup>\n                    Channels in Cardiac Myocytes Requires the Distal Carboxyl Terminus of α\n                    <sub>1C</sub>\n                    but Not Serine 1928"}]},{"@id":"https://cir.nii.ac.jp/crid/1364233271108763776","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"Unchanged β-Adrenergic Stimulation of Cardiac L-type Calcium Channels in Cav1.2 Phosphorylation Site S1928A Mutant Mice"}]},{"@id":"https://cir.nii.ac.jp/crid/1364233271120265600","@type":"Article","relationType":["references"],"jpcoar:relatedTitle":[{"@value":"β-Adrenergic Regulation of the L-type Ca\n            <sup>2+</sup>\n            Channel Does Not Require Phosphorylation of α\n            <sub>1C</sub>\n            Ser\n            <sup>1700</sup>"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1152/ajpcell.00267.2014"},{"@type":"KAKEN","@value":"PRODUCT-15071428"},{"@type":"OPENAIRE","@value":"doi_dedup___::3d5f74bbe075a573721b42e26612a72f"},{"@type":"CROSSREF","@value":"10.1152/ajpcell.00157.2015_references_DOI_9m48sU9mNNM03PdrBXT6fZ4ntMg"},{"@type":"CROSSREF","@value":"10.1016/j.jphs.2018.05.010_references_DOI_9m48sU9mNNM03PdrBXT6fZ4ntMg"},{"@type":"CROSSREF","@value":"10.1113/jp273736_references_DOI_9m48sU9mNNM03PdrBXT6fZ4ntMg"},{"@type":"CROSSREF","@value":"10.1152/ajpcell.00426.2018_references_DOI_9m48sU9mNNM03PdrBXT6fZ4ntMg"},{"@type":"CROSSREF","@value":"10.1016/j.jphs.2017.03.002_references_DOI_9m48sU9mNNM03PdrBXT6fZ4ntMg"}]}