Protein SUMOylation in neuropathological conditions

D Anderson, KA Wilkinson, JM Henley

Research output: Contribution to journalArticle (Academic Journal)peer-review

29 Citations (Scopus)

Abstract

Small ubiquitin-related modifier (SUMO) proteins are ∼ 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.
Translated title of the contributionProtein SUMOylation in neuropathological conditions
Original languageEnglish
Pages (from-to)255 - 265
Number of pages11
JournalDrugs News and Perspectives
Volume22(5)
DOIs
Publication statusPublished - Jun 2009

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