The Israel Society for Neuroscience (ISFN) was founded in 1993 by a group of Israeli leading scientists conducting research in the area of neurobiology. The primary goal of the society was to promote and disseminate the knowledge and understanding acquired by its members, and to strengthen interactions between them. Since then, the society holds its annual meeting every year in Eilat during the month of December. At these annual meetings the senior Israeli neurobiologists, their teams, and their graduate students, as well as foreign scientists and students, present their recent research findings in platform and poster presentations. The meeting also offers the opportunity for the researchers to exchange information with each other, often leading to the initiation of collaborative studies. Both the number of members of the society and of those participating in the annual meeting is constantly increasing, and it is anticipated that this year about 600 scientists will convene at the Princess Hotel in Eilat, Israel. Further information concerning the Israel Society for Neuroscience can be found at http://www.isfn.org.il. Committee: Zvi Wollberg (President) Tel Aviv University Edi Barkai University of Haifa Etti Grauer Israel Institute for Biological Research, Ness Ziona Yoram Rami Grossman Ben Gurion University of the Negev Yoel Yaari Hebrew University of Jerusalem Gal Yadid Bar-Ilan University Shlomo Rotshenker (President Elect) Hebrew University of Jerusalem Ettie Grauer (Treasurer) Israel Institute for Biological Research, Ness Ziona Michal Gilady (Administrator) Rishon Le Zion

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 alphaCaMKII 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.