Abstract
The post-translational modification of proteins by members of the Small Ubiquitin-like MOdifier (SUMO) family is beginning to emerge as a key regulator of neuronal function. SUMO conjugation modifies the interaction of target proteins with protein partners, and thereby alters their subcellular localization, activity and stability. Importantly, SUMOylation is readily reversible, allowing cells to respond rapidly to varying cellular demands. SUMO has already been implicated in the regulation of multiple neuronal signalling pathways, mitochondrial dynamics, spine formation and synaptogenesis, as well as the direct control of neuronal excitability via its modulation of cell surface receptors and ion channels. Here, we outline the basic mechanics of the SUMO pathway, review major recent advances in the field and discuss the far-reaching implications of neuronal SUMOylation in health and disease.
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