The RNF10 protein interacts with the GluN2A subunit of the NMDA-type Glutamate receptor

Modulation of NMDA subunits composition is determinant for the biophysical properties, synaptic transmission and important for synaptic plasticity. In developing neurons NMDA GluN2B subunit is abundant, whereas mature neurons express more GluN2A subunit. Modulation of synaptic localization of GluN2A is not completely clarified, thus we explored new interaction partners for this NMDAR subunit. Through yeast two hybrid screening we found that Ring Finger Protein 10 (RNF10) interacts with GluN2A c-terminal tail. Thus, the main objective will be to study the interaction between GluN2A and RNF10 in hippocampal neurons and determinate its consequence in the synaptic function. Our data shows for first time the localization of RNF10 in hippocampal neurons, which is present in postsynaptic density. Also we found that RNF10 co-localizes with PSD-95 and preliminary data shows GluN2A, but not GluN2B, c-terminal interacts with RNF10. On the other hand we observed that RNF10 localization is modify by synaptic activity, where BCC treatments concentrate RNF10 at the nucleus. Our results suggest that RNF10 has a roll in the synaptic activity process which remain to be elucidated