PKC SUMOylation inhibits the binding of 14–3–3τ to GluK2 |
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| Authors: | Xiaoling Li Aoxue Zhu Jie Zhou |
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| Institution: | 1. Department of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory for Tumor Microenvironment and Inflammation, Institute of Medical Sciences, Shanghai Jiao Tong University School of Medicine, Shanghai, China;2. Department of Pharmacy, Renji Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China |
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| 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 14–3–3τ 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 14–3–3τ and GluK2a-containing receptors. Here we report that SUMOylation of PKC, but not GluK2, represses the binding of 14–3–3τ 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. |
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| Keywords: | 14–3–3τ GluK2 phosphorylation PKC SUMOylation |
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