Aryl hydrocarbon receptor-interacting protein (AIP)

Aryl hydrocarbon receptor-interacting protein (AIP) is a cytoplasmic, immunophilin-like co-chaperone protein critical for the stability and regulation of the aryl hydrocarbon receptor (AHR) complex. It contains an N-terminal peptidyl-prolyl cis-trans isomerase (PPIase) domain and tetratricopeptide repeats (TPRs) at the C-terminus, allowing it to scaffold AHR and the heat shock protein Hsp90, thereby preventing AHR degradation and regulating its cytoplasmic retention and activation. AIP acts as a tumor suppressor gene, notably in the pituitary, but displays diverse cellular functions in immunity and cell growth regulation across tissues. Loss-of-function mutations in AIP lead to a predisposition to early-onset and aggressive pituitary adenomas. AIP is not directly targeted by drugs but is a critical molecular scaffold influencing AHR signaling, xenobiotic metabolism, immune cell activation, and potentially cancer biology[1][2][3][4][5].

Other names

XAP2XAP-2ARA9FKBP16FKBP37Immunophilin homolog ARA9hepatitis B virus X-associated cellular protein 2aryl hydrocarbon receptor-associated protein 9FKBP prolyl isomerase 16X-associated protein-2FK506-binding protein 37Ah receptor activated 9PITA1SMTPHNHBV X-associated protein 2

Not a direct drug target; functions as a co-chaperone modulator of AHR pathway and is not directly targeted by drugs[2][5].