title: Two phosphorylation sites on eIF-2 alpha.
abstract: Protein synthesis in mammalian cells can be regulated through phosphorylation/dephosphorylation of the alpha subunit of initiation factor 2, eIF-2. Two specific kinases have been identified that apparently phosphorylate the same site(s). Controversy exists as to whether serine-48 is a phosphorylation site in addition to serine-51. A recent publication is discussed that, in this author's view, answers the question of the phosphorylation sites. It is suggested that phosphorylation proceeds sequentially with serine-51 being the first and serine-48 the second phosphorylation site. Phosphorylation of both sites is required for inhibition of protein synthesis.
authors.affiliation: Department of Chemistry, University of Texas, Austin 78712.
authors.forename: G
authors.initials: G
authors.lastname: Kramer
mesh_terms: D001665:Binding Sites; D015852:Eukaryotic Initiation Factor-2 / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D009154:Mutation; D010766:Phosphorylation; D014176:Protein Biosynthesis; D012694:Serine
chemical_list: D015852:Eukaryotic Initiation Factor-2; D012694:Serine