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The Role of Protein SUMOylation in Neuronal Function

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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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Acknowledgements

Work in the lab of JMH is funded by the MRC, the Wellcome Trust, the ERC and the BBSRC. We thank Atsushi Nishimune for invaluable guidance, discussion and advice.

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  1. Department of Anatomy MRC Centre for Synaptic Plasticity, School of Biochemistry, University of Bristol, University Walk, Medical Sciences Building, Bristol, BS8 1TD, UK

    Jeremy M. Henley

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  1. Kevin A. Wilkinson
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  2. Jeremy M. Henley
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Correspondence to Jeremy M. Henley .

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  1. School of Biological Sciences, University of Southampton, Life Science Building (B85), SO17 1BJ, Southampton, SO16 7PX, United Kingdom

    Andreas Wyttenbach

  2. School of Biological Sciences, University of Southampton, Life Science Building (B85), SO17 1BJ, Southampton, SO16 7PX, United Kingdom

    Vincent O'Connor

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Wilkinson, K.A., Henley, J.M. (2011). The Role of Protein SUMOylation in Neuronal Function. In: Wyttenbach, A., O'Connor, V. (eds) Folding for the Synapse. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-7061-9_9

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