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Multiple Choice
When protein kinase A (PKA) is inactive, which of the following best describes its state?
A
PKA is bound to cAMP, leading to activation of its catalytic subunits.
B
The catalytic subunits are free and actively phosphorylating target proteins.
C
PKA is degraded by proteasomes in the cytoplasm.
D
The regulatory and catalytic subunits are bound together, preventing substrate phosphorylation.
Verified step by step guidance
1
Understand the structure of protein kinase A (PKA): PKA is a holoenzyme composed of two regulatory subunits and two catalytic subunits. When inactive, these subunits are bound together.
Recognize the role of the regulatory subunits: The regulatory subunits inhibit the activity of the catalytic subunits by physically blocking their ability to phosphorylate target proteins.
Learn the activation mechanism: PKA becomes active when cyclic AMP (cAMP) binds to the regulatory subunits. This binding causes a conformational change, releasing the catalytic subunits.
Clarify the inactive state: In the absence of cAMP, the regulatory and catalytic subunits remain bound together, preventing the catalytic subunits from phosphorylating substrates.
Conclude the correct description: The inactive state of PKA is best described as the regulatory and catalytic subunits being bound together, which prevents substrate phosphorylation.