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    eEF2K tagged posts

    Connection found between Memory Mechanisms, Resistance to Epilepsy

    November 27, 2016, Categories  Biology/Biotechnology, Health/Medical

    eEF2 pathways regulate cellular protein translation. (A) Activation of NMDA receptor enables Ca2+ to enter the cell. In the presence of Ca2+ and calmodulin (CaM) elongation factor 2 kinase (eEF2K) is activated, leading to increased phosphorylation (and inhibition) of elongation factor 2 (eEF2) and overall decreased protein translation. (B) Protein kinase A (PKA) can phosphorylate eEF2K, thereby reducing eEF2K dependency on calmodulin and Ca2+, making eEF2K more active. In the presence of calmodulin and Ca2+, eEF2K inhibits eEF2 activity by phosphorylation, which results in attenuated cap-dependent translation, but evidently, can increase translation of other proteins like Arc, BDNF, and, αCAMKII. (C) Possible mTOR pathway for translation regulation. mTOR can regulate eEF2 phosphorylation and, consequently, elongation by phosphorylation of S6K1 for example, which can then inhibit eEF2K activity by phosphorylation (different phosphorylation site from PKA), leading to decreased phospho-eEF2 levels and increased elongation rate.

    eEF2 pathways regulate cellular protein translation

    A new study exposes a new biological mechanism that, on the one hand, damages a very specific type of memory, but at the same time provides resistance to epilepsy. Research student Elham Taha from the laboratory of Prof. Kobi Rosenblum explains: “In both healthy and sick brains, the relationship between the activities of the nerve cells that cause the transfer of information and activities delaying the transmission of information is extremely important. We know that damage to this relationship forms the basis of various brain diseases, such as neuro-developmental diseases and epilepsy. The aim of our study was to isolate molecular components that serve the creation of long-term memories...

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