Disease relevance of PAIP1

• Paip2 preferentially inhibits translation of a poly(A)-containing mRNA, but has no effect on the translation of hepatitis C virus mRNA, which is cap- and eIF4G-independent [1].

High impact information on PAIP1

• Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation [2].
• Here, we describe a new human PABP-interacting protein, PAIP-I, whose sequence is similar to the central portion of eIF4G and which interacts with eIF4A [2].
• Overexpression of PAIP-1 in COS-7 cells stimulates translation, perhaps by providing a physical link between the mRNA termini [2].
• Translational repression by a novel partner of human poly(A) binding protein, Paip2 [1].
• We have determined the solution structure of the human PABC domain in complex with two peptides from PABP-interacting protein-1 (Paip1) and Paip2 [3].

Biological context of PAIP1

• PABP also contains two Paip1 binding sites, one located in RNA recognition motifs 1 and 2 and the other located in the C-terminal domain [4].
• Fructose modulates GLUT5 mRNA stability in differentiated Caco-2 cells: role of cAMP-signalling pathway and PABP (polyadenylated-binding protein)-interacting protein (Paip) 2 [5].

Associations of PAIP1 with chemical compounds

• To study the mechanism of the Paip1-PABP interaction, far-Western, glutathione S-transferase pull-down, and surface plasmon resonance experiments were performed [4].

Physical interactions of PAIP1

• PABP-interacting protein 1 (Paip1) is another factor that interacts with PABP to coactivate translation [1].

References