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Phosphorylation of translation initiation factor eIF 2α at Ser51 depends on site‐ and context‐specific information
Author(s) -
Uppala Jagadeesh Kumar,
Ghosh Chandrima,
Sathe Leena,
Dey Madhusudan
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13214
Subject(s) - phosphorylation , eukaryotic translation , translation (biology) , kinase , initiation factor , biochemistry , context (archaeology) , microbiology and biotechnology , chemistry , biology , messenger rna , gene , paleontology
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 eIF 2α and downregulates cellular protein synthesis. Structural information on eIF 2α 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.