PROTEIN SUMOYLATION IN NEUROPATHOLOGICAL CONDITIONS

被引:35
作者
Anderson, Dina B. [1 ]
Wilkinson, Kevin A. [1 ]
Henley, Jeremy M. [1 ]
机构
[1] Univ Bristol, MRC, Ctr Synapt Plast, Dept Anat,Sch Med Sci,Univ Walk, Bristol BS8 1TD, Avon, England
基金
英国生物技术与生命科学研究理事会; 英国惠康基金;
关键词
INTRANUCLEAR INCLUSION DISEASE; UBIQUITIN-PROTEASOME SYSTEM; AMYLOID PRECURSOR PROTEIN; FOCAL CEREBRAL-ISCHEMIA; THYMINE-DNA GLYCOSYLASE; NUCLEAR-PORE COMPLEX; KAPPA-B ACTIVATION; ALPHA-SYNUCLEIN; SUMO-1; MODIFICATION; COVALENT MODIFICATION;
D O I
10.1358/dnp.2009.22.5.1378636
中图分类号
R9 [药学];
学科分类号
100702 [药剂学];
摘要
Small ubiquitin-related modifier (SUMO) proteins are similar to 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.
引用
收藏
页码:255 / 265
页数:11
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