Repair of isoaspartate formation modulates the interaction of deamidated 4E-BP2 with mTORC1 in brain.

ABSTRACT: In eukaryotes, a rate-limiting step of translation initiation is recognition of the mRNA 5' m(7)GpppN cap structure by the eukaryotic initiation factor 4F (eIF4F), a heterotrimeric complex consisting of the cap-binding protein, eIF4E, along with eIF4G, and eIF4A. The eIF4E-binding proteins (4E-BPs) repress translation by disrupting eIF4F formation, thereby preventing ribosome recruitment to the mRNA. Of the three 4E-BPs, 4E-BP2 is the predominant paralog expressed in the mammalian brain and plays an important role in synaptic plasticity and learning and memory. 4E-BP2 undergoes asparagine deamidation, solely in the brain, during early postnatal development. Deamidation spontaneously converts asparagines into a mixture of aspartates or isoaspartates, the latter of which may be destabilizing

SUBMITTER: Bidinosti M 

PROVIDER: S-EPMC2885220 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature