Protein kinase C-related kinase 2 phosphorylates the protein synthesis initiation factor eIF4E in starfish oocytes.
作者： Shyh-Jye Lee , Genevieve Stapleton , Julia H. Greene , Merrill B. Hille
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摘要: Phosphorylation of eIF4E is required for protein synthesis during starfish oocyte maturation. The activity kinase C-related 2 (PRK2) increases prior to the phosphorylation (G. Stapleton et al., 1998, Dev. Biol. 193, 34–46). We investigate here whether activated by PRK2. A 3.5-kb clone isolated from cDNA 57% identical human and contains putative site serine-209. serine-209 environment (SKTGS209MAKSRF) similar consensus sequence C related kinases. fusion (GST-4E) was phosphorylated in vitro PRK2 presence 1,2-diolyl-sn-glycerol 3-phosphate. In contrast, replacing GST-4E with an alanine significantly reduced this phosphorylation. Analysis two-dimensional phosphopeptide mapping reveals a major trypsin-digested GST-4E, but not its mutant. Importantly, corresponds 32P-labeled oocytes. Thus, may regulate translation initiation maturation phosphorylating residue starfish. also demonstrate that high levels cAMP inhibit activation PRK2, eIF4E, binding maturation, while PI3 activates these proteins.
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