PRKAR1B Antibody – Rabbit Polyclonal

Cyclic AMP-dependent protein kinase A (PKA) is an essential enzyme in the signaling pathway of the second messenger cAMP. Through phosphorylation of target proteins, PKA controls many biochemical events in the cell including regulation of metabolism, ion transport, and gene transcription. The PKA holoenzyme is composed of 2 regulatory and 2 catalytic subunits and dissociates from the regulatory subunits upon binding of cAMP.[supplied by OMIM, Jun 2009]

Function: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Ref.9

Subunit structure: The inactive holoenzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP releases the two active catalytic monomers and the regulatory dimer. Interacts with PRKX; regulates this cAMP-dependent protein kinase. Interacts with C2orf88/smAKAP; this interaction may target PRKAR1B to the plasma membrane. Ref.9 Ref.10

Subcellular location: Cell membrane Ref.10.

Tissue specificity: Four types of regulatory chains are found: I-alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible.

Post-translational modification: The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity.

Sequence similarities: Belongs to the cAMP-dependent kinase regulatory chain family.Contains 2 cyclic nucleotide-binding domains.