title: Phosphorylation of eIF4E at a conserved serine in Aplysia.
abstract: We have cloned eIF4E from the marine mollusk, Aplysia californica. The sequence of eIF4E from Aplysia is more similar to vertebrate eIF4Es than to other invertebrate sequences. Aplysia eIF4E is encoded by two tissue-specific RNAs. Antibodies raised to the carboxyl terminus of eIF4E recognize a 29-kDa protein that can bind to 7-methyl-GTP caps. The phosphorylation site identified in mammalian eIF4E is conserved in the Aplysia homologue, and an Aplysia eIF4E fusion protein is phosphorylated well by both Aplysia protein kinase C isoforms. However, protein kinase C phosphorylates both Ser-207 and Thr-208 in vitro, while only Ser-207 is phosphorylated in vivo. We have confirmed that Ser-207 is phosphorylated in vivo by raising a phosphopeptide antibody to this site. This antibody will be useful in determining the signal transduction pathways leading to eIF4E phosphorylation in Aplysia.
authors.affiliation: Department of Neurology and Neurosurgery, McGill University, Montreal Neurological Institute, Montreal, Quebec H3A 2B4, Canada.
authors.forename: J R
authors.initials: JR
authors.lastname: Dyer
authors.forename: A M
authors.initials: AM
authors.lastname: Pepio
authors.forename: S K
authors.initials: SK
authors.lastname: Yanow
authors.forename: W S
authors.initials: WS
authors.lastname: Sossin
mesh_terms: D000818:Animals; D001048:Aplysia; D001483:Base Sequence; D017124:Conserved Sequence; D017931:DNA Primers; D039561:Eukaryotic Initiation Factor-4E; D008969:Molecular Sequence Data; D010448:Peptide Initiation Factors / Q000737:chemistry / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D012694:Serine / Q000378:metabolism*
chemical_list: D017931:DNA Primers; D039561:Eukaryotic Initiation Factor-4E; D010448:Peptide Initiation Factors; D012694:Serine; D011493:Protein Kinase C