PKC SUMOylation inhibits the binding of 14–3–3τ to GluK2

Abstract

Phosphorylation and SUMOylation of the kainate receptor (KAR) subunit GluK2 have been shown to regulate KAR surface expression, trafficking and synaptic plasticity. In addition, our previous study has shown that a phosphorylation-dependent interaction of 14-3-3t and GluK2a-containing receptors contributes to the slow decay kinetics of native KAR-EPSCs. However, it is unknown whether SUMOylation participates in the regulation of the interaction between 14-3-3t and GluK2a-containing receptors. Here we report that SUMOylation of PKC, but not GluK2, represses the binding of 14-3-3t to GluK2a via decreasing the phosphorylation level of GluK2a. These results suggest that PKC SUMOylation is an important regulator of the 14-3-3 and GluK2a protein complex and may contribute to regulate the decay kinetics of KAR-EPSCs.

SUMOylation of synaptic and synapse‐associated proteins: An update

“…More recently, the same group also reported that SUMOylation of PKC inhibits the binding of 14–3‐3tau to GluK2 by reducing GluK2 phosphorylation (Li, Wang, Zhu, Zhou, & Li, 2017). 14–3‐3tau is a conserved family of regulatory proteins that bind to a wide range of targets, and binding to GluK2 contributes to the slow decay kinetics of KAR‐mediated excitatory post‐synaptic currents (EPSCs) (Sun et al., 2013).…”