Reference: Uppala JK, et al. (2018) Phosphorylation of translation initiation factor eIF2α at Ser51 depends on site- and context-specific information. FEBS Lett 592(18):3116-3125

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Abstract


Protein kinases phosphorylate specific amino acid residues of substrate proteins and regulate many cellular processes. Specificity for phosphorylation depends on the accessibility of these residues, and more importantly, kinases have preferences for certain residues flanking the phospho-acceptor site. Translation initiation factor 2α [eukaryotic translation initiation factor 2α (eIF2α)] kinase phosphorylates serine51 (Ser51) of eIF2α and downregulates cellular protein synthesis. Structural information on eIF2α reveals that Ser51 is located within a flexible loop, referred to as the Ser51 loop. Recently, we have shown that conformational change of the Ser51 loop increases the accessibility of Ser51 to the kinase active site for phosphorylation. Here, we show that the specificity of Ser51 phosphorylation depends largely on its relative position in the Ser51 loop and minimally on the flanking residues.

Reference Type
Journal Article | Research Support, N.I.H., Extramural
Authors
Uppala JK, Ghosh C, Sathe L, Dey M
Primary Lit For
Eukaryotic translation initiation factor 2 complex

Interaction Annotations


Genetic Interactions

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Interactor Interactor Allele Assay Annotation Action Phenotype SGA score P-value Source Reference

Physical Interactions 1 entry for 2 genes

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InteractorInteractorAssayAnnotationActionModification
GCN2SUI2Biochemical Activitymanually curatedBait-Hitphosphorylated residue
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