PRKAR1A Protein, Mouse (sf9, His)

PRKAR1A protein serves as a regulatory subunit in the cAMP-dependent protein kinases, playing a pivotal role in mediating cellular responses to cAMP signaling. The inactive holoenzyme comprises two regulatory chains and two catalytic chains. Upon activation by cAMP, the regulatory dimer dissociates, releasing two active catalytic monomers. PRKAR1A interacts with PRKACA and PRKACB, forming a dynamic complex involved in cAMP-dependent signaling cascades. Notably, it associates with RFC2, suggesting a potential role in cell survival mechanisms. Additional interactions include AKAP4, facilitating intricate signaling events, and RARA, where the interaction, influenced by cAMP or FSH, regulates RARA transcriptional activity. PRKAR1A further engages with phosphorylated PJA2, PRKX, CBFA2T3, and smAKAP, contributing to the modulation of cAMP-dependent protein kinase functions and targeting PRKAR1A to specific cellular locations, such as the plasma membrane. Additionally, PRKAR1A exhibits interactions with AICDA, indicating a role in diverse cellular processes. These interactions underscore the multifaceted involvement of PRKAR1A in cellular signaling and regulation.