title: Protein SUMOylation in neuropathological conditions.
abstract: Small ubiquitin-related modifier (SUMO) proteins are approximately 11 kDa proteins that can be covalently conjugated to lysine residues in defined target proteins. The resultant post-translational modification, SUMOylation, is vital for the viability of mammalian cells and regulates, among other things, a range of essential nuclear processes. It has become increasingly apparent in recent years that SUMOylation also serves multiple functions outside the nucleus and that it plays a critical role in the regulation of neuronal integrity and synaptic function. In particular, dysfunction of the SUMOylation pathway has been implicated in the molecular and cellular dysfunction associated with neurodegenerative and psychiatric disorders. Here, we outline current knowledge of the SUMO pathway and discuss the growing evidence for its involvement in multiple neurodegenerative disorders, with a view to highlighting the potential of the SUMO pathway as a putative drug target.
authors.affiliation: Medical Research Council Centre for Synaptic Plasticity, University of Bristol, Bristol BS8 1TD, UK.
authors.forename: Dina B
authors.initials: DB
authors.lastname: Anderson
authors.forename: Kevin A
authors.initials: KA
authors.lastname: Wilkinson
authors.forename: Jeremy M
authors.initials: JM
authors.lastname: Henley
mesh_terms: D000818:Animals; D001921:Brain / Q000378:metabolism / Q000503:physiopathology; D016503:Drug Delivery Systems; D006801:Humans; D009422:Nervous System Diseases / Q000188:drug therapy / Q000503:physiopathology*; D020033:Protein Isoforms; D011499:Protein Processing, Post-Translational; D025841:Small Ubiquitin-Related Modifier Proteins / Q000378:metabolism*
chemical_list: D020033:Protein Isoforms; D025841:Small Ubiquitin-Related Modifier Proteins