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Regulation of Eukaryotic Initiation Factor 4E Phosphorylation in the Nervous System of Aplysia californica
Author(s) -
Dyer John R,
Sossin Wayne S
Publication year - 2000
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.2000.0750872.x
Subject(s) - aplysia , eif4e , phosphorylation , biology , protein kinase a , microbiology and biotechnology , protein phosphorylation , kinase , p38 mitogen activated protein kinases , biochemistry , translation (biology) , neuroscience , messenger rna , gene
We have used an antibody that specifically recognizes eukaryotic initiation factor 4E (eIF4E) when it is phosphorylated at Ser 207 to characterize eIF4E phosphorylation in the nervous system of Aplysia . The level of phosphorylated eIF4E, but not the level of total eIF4E, was significantly correlated with the basal rate of translation measured from different animals. Serotonin (5‐HT), a transmitter that regulates the rate of translation in Aplysia neurons, had mixed effects on eIF4E phosphorylation. 5‐HT decreased eIF4E phosphorylation in sensory cell clusters through activation of protein kinase C. 5‐HT increased eIF4E phosphorylation in the whole pleural ganglia. In the Aplysia nervous system, eIF4E phosphorylation correlated with phosphorylation of the p38 MAP kinase, but not the p42 MAP kinase (ERK). Furthermore, an inhibitor of the p38 MAP kinase significantly decreased basal eIF4E phosphorylation, but an inhibitor of the MAP or ERK kinase (MEK) did not. Despite the correlation of eIF4E phosphorylation with the basal rate of translation, inhibition of eIF4E phosphorylation by an inhibitor of the p38 MAP kinase did not significantly decrease the rate of translation.