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- W2995948738 abstract "The translation initiation repressor 4E-BP2 is deamidated in the brain on asparagines N99/N102 during early postnatal brain development. This post-translational modification enhances 4E-BP2 association with Raptor, a central component of mTORC1 and alters the kinetics of excitatory synaptic transmission. We show that 4E-BP2 deamidation is neuron specific, occurs in the human brain, and changes 4E-BP2 subcellular localization, but not its disordered structure state. We demonstrate that deamidated 4E-BP2 is ubiquitinated more and degrades faster than the unmodified protein. We find that enhanced deamidated 4E-BP2 degradation is dependent on Raptor binding, concomitant with increased association with a Raptor-CUL4B E3 ubiquitin ligase complex. Deamidated 4E-BP2 stability is promoted by inhibiting mTORC1 or glutamate receptors. We further demonstrate that deamidated 4E-BP2 regulates the translation of a distinct pool of mRNAs linked to cerebral development, mitochondria, and NF-κB activity, and thus may be crucial for postnatal brain development in neurodevelopmental disorders, such as ASD." @default.
- W2995948738 created "2019-12-26" @default.
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- W2995948738 date "2019-12-01" @default.
- W2995948738 modified "2023-10-16" @default.
- W2995948738 title "Raptor-Mediated Proteasomal Degradation of Deamidated 4E-BP2 Regulates Postnatal Neuronal Translation and NF-κB Activity" @default.
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- W2995948738 doi "https://doi.org/10.1016/j.celrep.2019.11.023" @default.
- W2995948738 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6915327" @default.
- W2995948738 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31825840" @default.
- W2995948738 hasPublicationYear "2019" @default.
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