regulation of cAMP-dependent protein kinase activity

Definition

Target type: biologicalprocess

Any process that modulates the frequency, rate or extent of cAMP-dependent protein kinase activity. [GOC:obol]

The regulation of cAMP-dependent protein kinase (PKA) activity is a complex and finely tuned process that plays a crucial role in cellular signaling. PKA is a serine/threonine kinase that is activated by cAMP, a second messenger molecule produced in response to a variety of stimuli, including hormones, neurotransmitters, and growth factors. The basic regulatory mechanism of PKA involves the interaction of the catalytic and regulatory subunits. PKA is composed of two regulatory (R) subunits and two catalytic (C) subunits. In the inactive state, the R subunits bind to and inhibit the C subunits. This interaction prevents the C subunits from phosphorylating target proteins. When cAMP levels rise, cAMP binds to the R subunits, causing a conformational change that releases the C subunits from the complex. These released catalytic subunits are now free to phosphorylate target proteins, initiating downstream signaling pathways. The key elements involved in the regulation of PKA activity include: 1. cAMP: cAMP binding to the R subunits triggers the activation of PKA. 2. R subunits: These subunits bind to and inhibit the C subunits in the absence of cAMP. 3. C subunits: These subunits are the catalytic units responsible for phosphorylating target proteins. 4. A-kinase anchoring proteins (AKAPs): These proteins act as scaffolding molecules, tethering PKA to specific cellular compartments. AKAPs help to target PKA to specific substrates and create localized signaling microdomains. 5. Phosphatases: Phosphatases dephosphorylate the phosphorylated proteins, effectively reversing the action of PKA. The regulation of PKA activity is tightly controlled by a balance of these factors, ensuring precise and specific cellular responses to various stimuli.'
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Proteins (1)

Compounds (28)