Cyclic AMP Dependent Protein Kinases, also known as protein kinase A (PKA), are a class of enzymes that play a crucial role in numerous cellular processes by regulating the actions of other proteins in response to cyclic adenosine monophosphate (cAMP) signaling. They are a family of serine/threonine kinases that are activated when cAMP levels increase within the cell.
Cyclic AMP Dependent Protein Kinases are composed of two regulatory subunits and two catalytic subunits. In the absence of cAMP, the regulatory subunits inhibit the activity of the catalytic subunits. However, when cAMP binds to the regulatory subunits, a conformational change occurs which releases the catalytic subunits and allows them to phosphorylate target proteins. This phosphorylation can have various effects, including activation or inhibition of the target protein's activity.
Cyclic AMP Dependent Protein Kinases are involved in a wide range of cellular processes, including metabolism, gene expression, cell growth, and differentiation. They are crucial in cellular signaling pathways, such as the cAMP-dependent pathway, which is important for regulating the function of hormones and neurotransmitters.
Dysregulation of cyclic AMP Dependent Protein Kinases has been implicated in various diseases, including cancer, cardiovascular disorders, neurological disorders, and metabolic disorders. Therefore, they represent potential targets for therapeutic intervention.
In summary, cyclic AMP Dependent Protein Kinases are enzymes that play a vital role in cellular processes by regulating the activity of other proteins in response to cAMP signaling. Their activation leads to phosphorylation of target proteins, influencing their function and contributing to important cellular functions.
