<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>22(1)</volume><submitter>Oz S</submitter><pubmed_abstract>&lt;h4>Background&lt;/h4>The β-adrenergic augmentation of cardiac contraction, by increasing the conductivity of L-type voltage-gated Ca&lt;sub>V&lt;/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&lt;sup>2+&lt;/sup> influx. In cardiomyocytes, the core subunit of Ca&lt;sub>V&lt;/sub>1.2, Ca&lt;sub>V&lt;/sub>1.2α&lt;sub>1&lt;/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&lt;sub>V&lt;/sub>1.2α&lt;sub</pubmed_abstract><journal>BMC biology</journal><pagination>276</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11603854</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Tripartite interactions of PKA catalytic subunit and C-terminal domains of cardiac Ca&lt;sup>2+&lt;/sup> channel may modulate its β-adrenergic regulation.</pubmed_title><pmcid>PMC11603854</pmcid><pubmed_authors>Tsemakhovich V</pubmed_authors><pubmed_authors>Katz M</pubmed_authors><pubmed_authors>Chomsky-Hecht O</pubmed_authors><pubmed_authors>Bertinetti D</pubmed_authors><pubmed_authors>Sholokh A</pubmed_authors><pubmed_authors>Klussmann E</pubmed_authors><pubmed_authors>Dascal N</pubmed_authors><pubmed_authors>Pallien T</pubmed_authors><pubmed_authors>Vysochek L</pubmed_authors><pubmed_authors>Hirsch JA</pubmed_authors><pubmed_authors>Sharon T</pubmed_authors><pubmed_authors>Tripathy DR</pubmed_authors><pubmed_authors>Sasson G</pubmed_authors><pubmed_authors>Schulz-Christian M</pubmed_authors><pubmed_authors>Fecher-Trost C</pubmed_authors><pubmed_authors>Zuhlke K</pubmed_authors><pubmed_authors>Oz S</pubmed_authors><pubmed_authors>Keren-Raifman T</pubmed_authors><pubmed_authors>Watad B</pubmed_authors><pubmed_authors>Herberg FW</pubmed_authors><pubmed_authors>Flockerzi V</pubmed_authors><pubmed_authors>Weiss S</pubmed_authors><pubmed_authors>Subramaniam S</pubmed_authors></additional><is_claimable>false</is_claimable><name>Tripartite interactions of PKA catalytic subunit and C-terminal domains of cardiac Ca&lt;sup>2+&lt;/sup> channel may modulate its β-adrenergic regulation.</name><description>&lt;h4>Background&lt;/h4>The β-adrenergic augmentation of cardiac contraction, by increasing the conductivity of L-type voltage-gated Ca&lt;sub>V&lt;/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&lt;sup>2+&lt;/sup> influx. In cardiomyocytes, the core subunit of Ca&lt;sub>V&lt;/sub>1.2, Ca&lt;sub>V&lt;/sub>1.2α&lt;sub>1&lt;/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&lt;sub>V&lt;/sub>1.2α&lt;sub</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Nov</publication><modification>2026-06-01T06:43:48.524Z</modification><creation>2025-04-04T00:45:22.162Z</creation></dates><accession>S-EPMC11603854</accession><cross_references><pubmed>39609812</pubmed><doi>10.1186/s12915-024-02076-9</doi></cross_references></HashMap>