| Article ID | Journal | Published Year | Pages | File Type | 
|---|---|---|---|---|
| 8473527 | Journal of Molecular and Cellular Cardiology | 2018 | 12 Pages | 
Abstract
												In cardiomyocytes, βAR stimulation induces PKA-mediated phosphorylation of the PP2A regulatory subunit isoform B56δ at S573, which increases associated PP2A catalytic activity. This is likely to regulate the phosphorylation status of specific B56δ-PP2A substrates, which remain to be identified.
											Keywords
												CaMKIIβARcMyBP-ccTnIPP1PLBcardiac myosin binding protein-CpKaBNZPP2AARVMI-1β-Adrenergic signalingMOIISOIsoprenalinethreonineSerinePhosphatasePhosphorylationphospholambancardiac troponin ICardiomyocytesadult rat ventricular myocytesknock outwild typeprotein kinase AProtein kinase A (PKA)multiplicity of infectioncalcium/calmodulin-dependent kinase IIβ-Adrenergic receptor
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											Authors
												Antonella Ranieri, Elizabeth Kemp, Joseph R. Burgoyne, Metin Avkiran, 
											