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A molecular switch for translational control in taste memory consolidation
Author(s) -
Belelovsky K.,
Elkobi A.,
Kaphzan H.,
Nairn A. C.,
Rosenblum K.
Publication year - 2005
Publication title -
european journal of neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.346
H-Index - 206
eISSN - 1460-9568
pISSN - 0953-816X
DOI - 10.1111/j.1460-9568.2005.04428.x
Subject(s) - memory consolidation , phosphorylation , consolidation (business) , microbiology and biotechnology , neuroscience , protein phosphorylation , elongation factor , protein biosynthesis , biology , protein kinase a , chemistry , biochemistry , ribosome , rna , hippocampus , accounting , gene , business
In a variety of species memory consolidation following different learning paradigms has been shown to be dependent on protein synthesis. However, it is not known whether modulation of protein synthesis is a critical component of the consolidation process, nor is the identity of any protein(s) subject to translational regulation, known. We report here that phosphorylation of eukaryotic elongation factor‐2 (eEF2), an indicator for translational elongation attenuation, is correlated with input that produces taste memory consolidation in the relevant cortex of rat. The temporal pattern of eEF2 phosphorylation is similar to extra‐cellular regulated kinase 2 (ERK2) activation and S6K1 phosphorylation, which are known to stimulate translation initiation. In addition, increased eEF2 phosphorylation and increased αCaMKII expression is detected in a synaptoneurosomal fraction made from taste cortex following memory consolidation. These results suggest that increased initiation rate together with decreased elongation rate, during memory consolidation, shift the rate‐limiting step of protein synthesis, to produce a local switch‐like effect in the expression of neuronal proteins.