The Central Societies Committee (CSC) is the body responsible for student societies in Trinity College.

Small Ubiquitin-like MOdifier protein (SUMO) regulates transcriptional activity and the translocation of proteins across the nuclear membrane but little is known about the wider cellular role of protein SUMOylation. We have found a completely new role for protein SUMOylation in the regulation of kainate receptor endocytosis. We identified that SUMOylation of the kainate receptor GluR6 is necessary for agonist-dependent internalisation but not for internalisation per se. These findings, in turn, indicate an important role for SUMOylation in the modulation of synaptic transmission and synaptic plasticity. 

We anticipate that, like phosphorylation and ubiquitination, protein SUMOylation may have complex, varied and crucial roles in determining the fate of modified synaptic proteins and will have far reaching implications for the understanding of synaptic function.  In this wider context, synaptic protein SUMOylation is a new and exciting field of investigation. We are therefore investigating the roles of SUMOylation of a range of putative target proteins in normal and pathological synaptic transmission. SUMOylation has already been implicated in a diverse array of synaptopathies. Therefore, better understanding of the regulation and consequences of synaptic SUMOylation is of fundamental importance. 

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