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Protein Sumoylation in Brain Development, Neuronal Morphology and Spinogenesis

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Abstract

Small ubiquitin-like modifiers (SUMOs) are polypeptides resembling ubiquitin that are covalently attached to specific lysine residue of target proteins through a specific enzymatic pathway. Sumoylation is now seen as a key posttranslational modification involved in many biological processes, but little is known about how this highly dynamic protein modification is regulated in the brain. Disruption of the sumoylation enzymatic pathway during the embryonic development leads to lethality revealing a pivotal role for this protein modification during development. The main aim of this review is to briefly describe the SUMO pathway and give an overview of the sumoylation regulations occurring in brain development, neuronal morphology and synapse formation.

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Acknowledgments

We thank F. Aguila for excellent artwork. We gratefully acknowledge the ‘Fondation pour la Recherche Médicale’ (Equipe labellisée ‘Fondation pour la Recherche Médicale’ DEQ20111223747), the National Research Agency (ANR JCJC), the ‘Jérôme Lejeune’ and ‘Bettencourt-Schueller’ foundations for financial support. S.M. is a fellow from Young Investigator CNRS ATIP/ATIP+ and ANR JCJC programs. This work was also supported by the French Government through the ‘Investments for the Future,’ LabEx SIGNALIFE # ANR-11-LABX-0028-01.

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  1. Institut de Pharmacologie Moléculaire et Cellulaire, Laboratory of Excellence ‘Network for Innovation on Signal Transduction Pathways in Life Sciences’, UMR7275, Centre National de la Recherche Scientifique, University of Nice—Sophia-Antipolis, 660 route des lucioles, 06560, Valbonne, France

    Carole Gwizdek, Frédéric Cassé & Stéphane Martin

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  1. Carole Gwizdek
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  2. Frédéric Cassé
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  3. Stéphane Martin
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Correspondence to Stéphane Martin.

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Gwizdek, C., Cassé, F. & Martin, S. Protein Sumoylation in Brain Development, Neuronal Morphology and Spinogenesis. Neuromol Med 15, 677–691 (2013). https://doi.org/10.1007/s12017-013-8252-z

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  • DOI: https://doi.org/10.1007/s12017-013-8252-z

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