title: Protein SUMOylation in spine structure and function.
abstract: The active regulation of spine structure and function is of fundamental importance for information storage in the brain. Many proteins involved in spine development and activity-dependent remodelling are potential or validated substrates for modification by the Small Ubiquitin-like Modifier (SUMO). The functional consequences of neuronal protein SUMOylation appear diverse and, in many cases, have not yet been determined. However, for several proteins SUMOylation has been shown to be a key regulator, which has a profound impact on spine dynamics and protein trafficking and function. Here we provide an overview of neuronal SUMOylation and discuss how greater understanding of this relatively recently discovered posttranslational modification will provide insight into the complexity of protein interactions that control synaptic activity and dysfunction.
authors: MRC Centre for Synaptic Plasticity, School of Biochemistry Medical Sciences Building, University of Bristol, University Walk, Bristol, BS8 1TD, UK.
authors: Tim J
authors: TJ
authors: Craig
authors: Jeremy M
authors: JM
authors: Henley
mesh_terms: D000818:Animals; D001921:Brain / Q000166:cytology; D049229:Dendritic Spines / Q000502:physiology*; D008954:Models, Biological; D009474:Neurons / Q000166:cytology* / Q000648:ultrastructure; D025841:Small Ubiquitin-Related Modifier Proteins / Q000235:genetics / Q000378:metabolism*; D058207:Sumoylation / Q000502:physiology*; D013569:Synapses / Q000502:physiology* / Q000648:ultrastructure
chemical_list: D025841:Small Ubiquitin-Related Modifier Proteins