Measuring synaptic protein acetylation

JULIA BUSSO; ANGELES SALLES; MARIANO BOCCIA; RAMIRO FREUDENTHAL

Huerta Grande

Congreso; Congreso SAN 2014; 2014

SAN

During long term memory (LTM) consolidation, changes occur that affect the nervous system at different scales, and many of these changes take place at the inter-neuronal contact, the synapse. Different cellular and molecular mechanisms underlie the temporal phases of Memory: induction requires an increase in intracellular calcium, early persistence depends on post -translational modifications (PTM) and late stages need gene transcription and protein synthesis. Our aim is to study the lysine acetylation of synaptic proteins and their signaling pathway during long term memory consolidation in the hippocampus of the mouse. Reversible lysine acetylation affects mRNA stability, and the localisation, interaction, degradation and function of proteins, suggesting that this PTM may be responsible for some of the local changes that occur distal from the neuronal soma. Many non-histone proteins systems were found to be regulated by acetylatation, among them two are our focus: the acetylation of Tubulins (α and β) and its effects in protein transport, and the interaction between NF-kappa B and lysine acetyl transferases (KATs). Here we report the conditions