{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["22(1)"],"submitter":["Oz S"],"pubmed_abstract":["<h4>Background</h4>The β-adrenergic augmentation of cardiac contraction, by increasing the conductivity of L-type voltage-gated Ca<sub>V</sub>1.2 channels, is of great physiological and pathophysiological importance. Stimulation of β-adrenergic receptors (βAR) activates protein kinase A (PKA) through separation of regulatory (PKAR) from catalytic (PKAC) subunits. Free PKAC phosphorylates the inhibitory protein Rad, leading to increased Ca<sup>2+</sup> influx. In cardiomyocytes, the core subunit of Ca<sub>V</sub>1.2, Ca<sub>V</sub>1.2α<sub>1</sub>, exists in two forms: full-length or truncated (lacking the distal C-terminus (dCT)). Signaling efficiency is believed to emanate from protein interactions within multimolecular complexes, such as anchoring PKA (via PKAR) to Ca<sub>V</sub>1.2α<sub"],"journal":["BMC biology"],"pagination":["276"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11603854"],"repository":["biostudies-literature"],"pubmed_title":["Tripartite interactions of PKA catalytic subunit and C-terminal domains of cardiac Ca<sup>2+</sup> channel may modulate its β-adrenergic regulation."],"pmcid":["PMC11603854"],"pubmed_authors":["Tsemakhovich V","Katz M","Chomsky-Hecht O","Bertinetti D","Sholokh A","Klussmann E","Dascal N","Pallien T","Vysochek L","Hirsch JA","Sharon T","Tripathy DR","Sasson G","Schulz-Christian M","Fecher-Trost C","Zuhlke K","Oz S","Keren-Raifman T","Watad B","Herberg FW","Flockerzi V","Weiss S","Subramaniam S"],"additional_accession":[]},"is_claimable":false,"name":"Tripartite interactions of PKA catalytic subunit and C-terminal domains of cardiac Ca<sup>2+</sup> channel may modulate its β-adrenergic regulation.","description":"<h4>Background</h4>The β-adrenergic augmentation of cardiac contraction, by increasing the conductivity of L-type voltage-gated Ca<sub>V</sub>1.2 channels, is of great physiological and pathophysiological importance. Stimulation of β-adrenergic receptors (βAR) activates protein kinase A (PKA) through separation of regulatory (PKAR) from catalytic (PKAC) subunits. Free PKAC phosphorylates the inhibitory protein Rad, leading to increased Ca<sup>2+</sup> influx. In cardiomyocytes, the core subunit of Ca<sub>V</sub>1.2, Ca<sub>V</sub>1.2α<sub>1</sub>, exists in two forms: full-length or truncated (lacking the distal C-terminus (dCT)). Signaling efficiency is believed to emanate from protein interactions within multimolecular complexes, such as anchoring PKA (via PKAR) to Ca<sub>V</sub>1.2α<sub","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Nov","modification":"2026-06-01T06:43:48.524Z","creation":"2025-04-04T00:45:22.162Z"},"accession":"S-EPMC11603854","cross_references":{"pubmed":["39609812"],"doi":["10.1186/s12915-024-02076-9"]}}