cAMP-dependent protein kinase type I regulatory subunit (PRKAR1 (with type-specific gene names PRKAR1A and PRKAR1B))

cAMP-dependent protein kinase type I regulatory subunit (PRKAR1) is a core component of the **protein kinase A (PKA)** holoenzyme, which is a tetramer consisting of two regulatory and two catalytic subunits[2][3][6][7]. The regulatory type I subunits (either alpha, encoded by PRKAR1A, or beta, encoded by PRKAR1B) bind cAMP molecules, leading to conformational changes that release the catalytic subunits and activate downstream phosphorylation cascades. These processes are central to numerous cellular responses including metabolism, gene expression, cell cycle, and hormonal signaling. Mutations and dysregulation of PRKAR1 subunits are implicated in various diseases, especially endocrine tumors (such as those seen in Carney complex), as well as in certain cancers and neurological disorders[2][5][7]. The PKA system as a whole is a well-established signal transduction hub, but the regulatory subunits themselves are not generally direct drug targets; rather, they are modulated via pathways that control cellular cAMP levels, for which several pharmacological agents exist.

Other names

Protein kinase A regulatory subunit type IPKA R1cAMP-dependent protein kinase regulatory subunit type I-alpha (PRKAR1A)cAMP-dependent protein kinase regulatory subunit type I-beta (PRKAR1B)PKR1

Modulation of cAMP-mediated signaling via competition with cAMP for regulatory subunit binding, release or sequestration of catalytic subunits to alter phosphorylation pathways