A-kinase-interacting protein 1 (AKIP1)

A-kinase-interacting protein 1 (AKIP1) is a proline-rich scaffold protein first identified in breast and prostate cancer cell lines. AKIP1 modulates interactions between protein kinase A (PKA) and other cellular signaling proteins. It is known to regulate both nuclear (gene transcription via NF-κB) and mitochondrial functions (apoptosis, mitochondrial integrity)[1][2]. AKIP1’s expression is upregulated in cardiac cells under oxidative and ischemic stress, where it localizes primarily to mitochondria and promotes survival through interactions with proteins such as apoptosis-inducing factor (AIF) and heat shock protein 70 (Hsp70)[1]. AKIP1 acts as a molecular bridge or scaffold: it connects PKA to the NF-κB transcription factor (p65), modulating NF-κB-dependent gene transcription, which is important for cell survival and anti-apoptotic signaling; its effects depend on its expression level and the cell type[2]. Its significance as a therapeutic target is under investigation, especially for limiting myocardial damage after ischemic injury and potentially supporting cancer treatment via modulation of cell survival pathways. Overall, AKIP1 functions as an integrator of stress response signaling—modulating PKA, gene transcription, mitochondrial function, and apoptosis in both the nucleus and mitochondria[1][2].

Other names

BCA3C11orf17Breast cancer-associated gene 3 proteinPKA-interacting proteinProline-rich protein BCA3A kinase (PRKA) interacting protein 1koyt binding protein 1koyt binding protein 2koyt binding protein 3

Not applicable; AKIP1 is a scaffold/adaptor, not a direct target of traditional inhibitory or stimulatory drugs. Modulators of PKA signaling can alter AKIP1’s downstream effects.