Recombinant Human PRKAR1A protein

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The protein PRKAR1A also known as Protein Kinase A (PKA) type I-alpha regulatory subunit acts as a regulatory subunit of the cAMP-dependent protein kinase (PKA) enzyme. It exhibits an approximate mass of 42 kDa. PRKAR1A plays a role in modulating the enzyme's activity by binding to cAMP which causes the dissociation of the regulatory subunit and activation of the catalytic subunit. PRKAR1A is broadly expressed in many tissues including the thyroid heart and adrenal glands indicating its widespread physiological importance.

Biological function summary

The regulatory subunit type I-alpha influences processes by deactivating the catalytic subunit to maintain appropriate levels of enzyme activity. It engages in forming a functional holoenzyme complex with the catalytic subunits of PKA. This mechanistic interaction impacts various cellular functions such as cell growth metabolism and gene transcription highlighting the broad biological impact of PRKAR1A.

Pathways

The protein PRKAR1A plays a role in the cAMP signaling pathway and the MAPK/ERK pathway. In the cAMP pathway it partners with the catalytic subunits of PKA to regulate cellular responses to fluctuating levels of cAMP. The protein links with other PKA subunits and signaling molecules such as CREB to mediate physiological responses to extracellular stimuli therefore interfacing with multifaceted cellular pathways.

Alterations in PRKAR1A function are connected to Carney Complex a hereditary disease characterized by cardiac myxomas skin abnormalities and endocrine tumors. Mutations in PRKAR1A contribute to endocrine-related disorders like Cushing's syndrome. The protein relates to other proteins such as PKA catalytic subunits which may also undergo dysregulation highlighting PRKAR1A's influence in disease pathogenesis.