Polyadenylate-binding protein-interacting protein 2 (PAIP2)

Polyadenylate-binding protein-interacting protein 2 (PAIP2) is a translation repressor that binds to poly(A)-binding protein (PABP), interfering with the formation of the closed-loop structure of mRNA necessary for efficient translation initiation. PAIP2 competes with eIF4G for PABP, thus blocking PABP-mediated stimulation of translation and actively promoting dissociation of PABP from the poly(A) tail. By controlling PABP availability, PAIP2 negatively modulates both initiation and termination of protein synthesis; its function is phylogenetically conserved from flies to humans. Overproduction of PAIP2 can delay cell cycle progression and suppress oncogenic transformation, establishing it as a tumor suppressor. The intracellular levels of PAIP2 are regulated by ubiquitin-dependent degradation, linked to cell cycle and growth factor signaling. Disruption of PAIP2 regulation or function is implicated in cancer and potentially other diseases characterized by abnormally regulated translation. If additional specificity on drug interaction or biomarker utility is found in future data, these fields may be updated accordingly.

Other names

PAIP2AHSPC218PABP-interacting protein 2PAIP-2Poly(A)-binding protein-interacting protein 2PABC1-interacting protein 2polyA-binding protein-interacting protein 2

For hypothetical drugs: inhibition or modulation of PAIP2’s binding to PABP; restoration of translation repression in oncogenesis. Drugs targeting PAIP2 would likely act by influencing mRNA loop formation and translation initiation complex assembly