Paip1 interacts with poly(A) binding protein through two independent binding motifs.

@article{Roy2002Paip1IW,
  title={Paip1 interacts with poly(A) binding protein through two independent binding motifs.},
  author={Guylaine Roy and Gregory De Crescenzo and Kianoush Khaleghpour and Avak Kahvejian and Maureen D. O'Connor-McCourt and Nahum Sonenberg},
  journal={Molecular and cellular biology},
  year={2002},
  volume={22 11},
  pages={3769-82}
}
The 3' poly(A) tail of eukaryotic mRNAs plays an important role in the regulation of translation. The poly(A) binding protein (PABP) interacts with eukaryotic initiation factor 4G (eIF4G), a component of the eIF4F complex, which binds to the 5' cap structure. The PABP-eIF4G interaction brings about the circularization of the mRNA by joining its 5' and 3' termini, thereby stimulating mRNA translation. The activity of PABP is regulated by two interacting proteins, Paip1 and Paip2. To study the… CONTINUE READING
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