A molecular switch for translational control in taste memory consolidation

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) subjec...

Full description

Saved in:
Bibliographic Details
Published inThe European journal of neuroscience Vol. 22; no. 10; pp. 2560 - 2568
Main Authors Belelovsky, K., Elkobi, A., Kaphzan, H., Nairn, A. C., Rosenblum, K.
Format Journal Article
LanguageEnglish
Published Oxford, UK Blackwell Science Ltd 01.11.2005
Subjects
Online AccessGet full text
ISSN0953-816X
1460-9568
DOI10.1111/j.1460-9568.2005.04428.x

Cover

More Information
Summary: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.
Bibliography:ark:/67375/WNG-0DGR29B2-0
ArticleID:EJN4428
istex:86A96CB9F3D8FB47D026DACA93CB5E2D39A760CA
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0953-816X
1460-9568
DOI:10.1111/j.1460-9568.2005.04428.x