Mice hippocampal synaptic composition and non-histone protein acetylation

RIVAS S; ESQUIVEL L.; SALLES A; BUSSO J; KRAWCZYK MC; BAEZ V; BOCCIA MM; FREUDENTHAL R

CORDOBA

Congreso; XXXIV ANUAL MEETING SAN 2019; 2019

SAN

Protein acetylation is a post translational modification involved in gene transcription, DNA damage repair, cell division, protein folding and metabolism. The enzymes responsible for the transfer and removal of acetyl groups are lysine acetyltransferases (KAT) and lysine deacetylases (KDAC) respectively. KDACs are classified by its subcellular localization, principally nuclear or cytoplasmic. Protein acetylation affects synaptic plasticity and memory, but its effects on synaptic composition are poorly understood. There is evidence that proteinacetylation at synapse promotes the dendritic clustering of PSD95 in cultures of hippocampal neurons. In this study we found an increment of PSD95 clustering in mice hippocampal extracts after 45 minutes of inhibitory avoidance task respect to control animals. Moreover, an augmented level of non-histone protein lysine acetylation was found and it positively correlates with that of PSD95 in post synaptic densities, indicating a possibly causal relation. Similar results were found in primary culture of hippocampal neurons after chemical LTP. Finally, post training administration of Tubastatin A (an HDAC6 inhibitor) facilitates long-term memory consolidation after inhibitory avoidance task. These results strongly suggest that protein acetylation has an important role regulating the synaptic changes that occur during memory consolidation.