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SUMOylation is a post-translational modification that regulates protein signalling and complex formation by adjusting the conformation or protein-protein interactions of the substrate protein. There is a compelling and rapidly expanding body of evidence that, in addition to SUMOylation of nuclear proteins, SUMOylation of extranuclear proteins contributes to the control of neuronal development, neuronal stress responses and synaptic transmission and plasticity. In this brief review we provide an update of recent developments in the identification of synaptic and synapse-associated SUMO target proteins and discuss the cell biological and functional implications of these discoveries. © 2020 The Authors. Journal of Neurochemistry published by John Wiley & Sons Ltd on behalf of International Society for Neurochemistry.

Citation

Jeremy M Henley, Richard Seager, Yasuko Nakamura, Karolina Talandyte, Jithin Nair, Kevin A Wilkinson. SUMOylation of synaptic and synapse-associated proteins: An update. Journal of neurochemistry. 2021 Jan;156(2):145-161

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PMID: 32538470

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