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- W2594922842 abstract "The central role of protein kinases in controlling disease processes has spurred efforts to develop pharmaceutical regulators of their activity. A rational strategy to achieve this end is to determine intrinsic auto-regulatory processes, then selectively target these different states of kinases to repress their activation. Here we investigate auto-regulation of the innate immune effector protein kinase R, which phosphorylates the eukaryotic initiation factor 2α to inhibit global protein translation. We demonstrate that protein kinase R activity is controlled by auto-inhibition via an intra-molecular interaction. Part of this mechanism of control had previously been reported, but was then controverted. We account for the discrepancy and extend our understanding of the auto-inhibitory mechanism by identifying that auto-inhibition is paradoxically instigated by incipient auto-phosphorylation. Phosphor-residues at the amino-terminus instigate an intra-molecular interaction that enlists both of the N-terminal RNA-binding motifs of the protein with separate surfaces of the C-terminal kinase domain, to co-operatively inhibit kinase activation. These findings identify an innovative mechanism to control kinase activity, providing insight for strategies to better regulate kinase activity." @default.
- W2594922842 created "2017-03-16" @default.
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- W2594922842 date "2017-03-10" @default.
- W2594922842 modified "2023-09-23" @default.
- W2594922842 title "Auto-phosphorylation Represses Protein Kinase R Activity" @default.
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- W2594922842 doi "https://doi.org/10.1038/srep44340" @default.
- W2594922842 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5345052" @default.
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