- thiolester hydrolase activity
Catalysis of the reaction: RCO-SR' + H2O = RCOOH + HSR'. This reaction is the hydrolysis of a thiolester bond, an ester formed from a carboxylic acid and a thiol (i.e., RCO-SR'), such as that found in acetyl-coenzyme A.
- phospholamban complex
A protein complex found as a homopentamer of the phospholamban (PLN) protein in the sarcoplasmic reticulum (SR) membrane of cardiomyocytes. Cardiac PLN is a main determinant of muscle contraction and relaxation, by regulating intracellular calcium levels.
- adenylate cyclase-activating adrenergic receptor signaling pathway involved in cardiac muscle relaxation
An adrenergic receptor signaling pathway that contributes to a reduction in cardiac muscle contraction. Beta-adrenergic receptor-induced cardiac relaxation is achieved by a GPCR-activated adenylate cyclase generating cAMP; cAMP then activates the cAMP-dependent protein kinase A (PKA), which phosphorylates the sarcoplasmic reticulum (SR) membrane protein PLB. In its non-phosphorylated state, PLB acts as an inhibitor of the ATPase Ca(2+) pump of the cardiac SR (SERCA2a); inhibition of the pump is relieved upon phosphorylation. The pump removes Ca(2+) from the cytoplasm, thereby preventing cytosolic Ca(2+)-dependent activation of contractile proteins, leading to enhanced muscle relaxation.
- thioester metabolic process
The chemical reactions and pathways involving a thioester, a compound of general formula RC(=O)SR' in which the linking oxygen in an ester is replaced by a sulfur atom. They are the product of esterification between a carboxylic acid and a thiol.
- thioester biosynthetic process
The chemical reactions and pathways resulting in the formation of a thioester, a compound of general formula RC(=O)SR' in which the linking oxygen in an ester is replaced by a sulfur atom. They are the product of esterification between a carboxylic acid and a thiol.
- RS domain binding
Binding to an RS domain of a protein; RS domains are usually highly phosphorylated and characterized by the presence of arginine (R)/serine (S) dipeptides. The RS domain promotes protein-protein interactions and directs subcellular localization and, in certain situations, nucleocytoplasmic shuttling of individual SR proteins. They also play a role in splicing.