The PKA holoenzyme is a tetramer composed of two regulatory ® subunits and two catalytic © subunits. The regulatory subunits bind to cAMP, leading to the dissociation of the holoenzyme into a dimer of regulatory subunits bound to four cAMP molecules and two free monomeric catalytic subunits . This dissociation activates the catalytic subunits, which then phosphorylate various target proteins to elicit cellular responses.
PRKAR2A is one of the four regulatory subunits identified in humans. It can be phosphorylated by the activated catalytic subunit and interacts with various A-kinase anchoring proteins (AKAPs), determining the subcellular localization of PKA . This subunit is involved in regulating protein transport from endosomes to the Golgi apparatus and further to the endoplasmic reticulum (ER) .
cAMP-dependent protein kinase is essential for numerous cellular functions, including:
PRKAR2A, specifically, has been shown to regulate protein transport and is crucial for proper cellular signaling and function .
Mutations or dysregulation of PRKAR2A have been associated with various diseases, including:
Additionally, PRKAR2A is involved in pathways related to anti-inflammatory cytokine production and beta-2 adrenergic-dependent CFTR expression .
Recombinant human PRKAR2A is widely used in research to study its role in cellular signaling and disease mechanisms. Understanding the function and regulation of this protein can provide insights into developing therapeutic strategies for related diseases.